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1
Mizan, Muhammad Rauful, Desta Wirnas, NFN Tasliah, Nurul Hidayatun, and Joko Prasetiyono, S.P., M.Si. "Molecular Analysis and Phenotypic Performances of BC3F2 Upland Rice Lines Containing Alt and Pup1 Loci." Jurnal AgroBiogen 15, no. 2 (December 31, 2019): 83. http://dx.doi.org/10.21082/jbio.v15n2.2019.p83-92.
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<p>The challenges in upland rice cultivation are phosphorous (P) deficiency and aluminum (Al) toxicity, each controlled by Pup1 and Alt loci, respectively. Pyramiding the two genes into Indonesian rice varieties were previously done through Marker-Assisted Backcrossing method to obtain BC3F2 populations. The aims of this study were to analyze the BC3F2 upland rice lines containing the Alt and Pup1 loci molecularly (foreground and background analyses) and to test their phenotypic performances. Genetic materials tested included Dupa variety (donor of Alt) and three improved Indonesian genotypes (Dodokan-Pup1, Situ Bagendit-Pup1, and Batur-Pup1) as recurrent parents, Kasalath (donor of Pup1), and 300 BC3F2 lines from Dodokan-Pup1+Alt, Situ Bagendit-Pup1+Alt, and Batur-Pup1+Alt, respectively. The rice genotypes were selected individually using modified Yoshida nutrient solution, followed by foreground and background analyses. 150 out of 300 seedlings were selected and maintained until harvest in the greenhouse. Foreground analysis using markers (RM1361, RM12031, and Kas46-2) and tiller number performances resulted in 18 plants from BC3F2 Dodokan-Pup1+Alt, 30 plants from BC3F2 Situ Bagendit-Pup1+Alt, and 25 plants from BC3F2 Batur-Pup1+Alt still carrying Alt and Pup1 loci. Background analysis using molecular markers showed that the best individual lines of BC3F2 were number 56 for BC3F2 Dodokan-Pup1+Alt, number 32 or 70 for BC3F2 Situ Bagendit-Pup1+Alt, and number 20 for BC3F2 Batur-Pup1+Alt. The selected lines having both both Alt and Pup1 loci in homozygote condition with highest number of tiller per plant which are useful genetic materials for developing upland rice variety tolerance to low P and Al toxicity.</p>
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Shin, Na-Hyun, O. New Lee, Jae-Hyuk Han, Kihwan Song, Hee-Jong Koh, Soo-Cheul Yoo, and Joong Hyoun Chin. "The Effect of Water Level in Rice Cropping System on Phosphorus Uptake Activity of Pup1 in a Pup1+Sub1 Breeding Line." Plants 10, no. 8 (July 26, 2021): 1523. http://dx.doi.org/10.3390/plants10081523.
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Pyramiding useful QTLs into an elite variety is a promising strategy to develop tolerant varieties against multiple abiotic stresses. However, some QTLs may not be functionally compatible when they are introgressed into the same variety. Here, we tested the functional compatibility of Pup1 and Sub1, major QTLs for tolerance to phosphorus (P)-deficiency and submergence conditions, respectively. Phenotypic analysis revealed that IR64-Pup1+Sub1 (IPS) plants harboring both Pup1 and Sub1 QTLs show significant tolerance to submerged conditions, similarly to IR64-Sub1, while IPS failed to tolerate P deficiency and mild drought conditions; only IR64-Pup1 showed P deficiency tolerance. In submerged conditions, Sub1A and OsPSTOL1, major genes for Sub1 and Pup1 QTLs, respectively, were expressed at the same levels as in IPS and IR64-Sub1 and in IPS and IR64-Pup1, respectively. On the other hand, in P-non-supplied condition, crown root number, root length, and OsPSTOL1 expression level were significantly lower in IPS compared to those of IR64-Pup1. However, there was no significant difference in P content between IPS and IR64-Pup1. These results imply that Pup1 does not compromise Sub1 function in submerged condition, while Sub1 suppresses Pup1 function in P-non-supplied condition, possibly by regulating the transcript level of Pup1. In conclusion, Pup1 and Sub1 are regarded as functionally compatible under submergence condition but not under P-non-supplied condition. Further study is needed to elucidate the functional incompatibility of Pup1 and Sub1 QTLs in IPS under P-non-supplied condition.
3
Wang, S. S., and M. C. Brandriss. "Proline utilization in Saccharomyces cerevisiae: sequence, regulation, and mitochondrial localization of the PUT1 gene product." Molecular and Cellular Biology 7, no. 12 (December 1987): 4431–40. http://dx.doi.org/10.1128/mcb.7.12.4431.
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The PUT1 gene of Saccharomyces cerevisiae, believed to encode proline oxidase, has been completely sequenced and contains an open reading frame capable of encoding a polypeptide of 476 amino acids in length. The amino terminus of the protein deduced from the DNA sequence has a characteristic mitochondrial import signal; two PUT1-lacZ gene fusions were constructed that produced mitochondrially localized beta-galactosidase in vivo. The transcription initiation and termination sites of the PUT1 mRNA were determined. By using a PUT1-lacZ gene fusion that makes a cytoplasmic beta-galactosidase, the regulation of the PUT1 gene was studied. PUT1 is inducible by proline, responds only slightly to carbon catabolite repression, and is not regulated by the cytochrome activator proteins HAP1 and HAP2. The PUT1 gene is under oxygen regulation; expression in anaerobically grown cells is 10-fold lower than in aerobically grown cells. Oxygen regulation is abolished when cells are respiratory deficient. PUT1 expression in a [rho-] strain grown either aerobically or anaerobically is as high as that seen in a [rho+] strain grown aerobically. Studies on PUT1 promoter deletions define a region between positions -458 and -293 from the translation initiation site that is important for full expression of the PUT1 gene and required for oxygen regulation.
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Wang, S. S., and M. C. Brandriss. "Proline utilization in Saccharomyces cerevisiae: sequence, regulation, and mitochondrial localization of the PUT1 gene product." Molecular and Cellular Biology 7, no. 12 (December 1987): 4431–40. http://dx.doi.org/10.1128/mcb.7.12.4431-4440.1987.
Full textAbstract:
The PUT1 gene of Saccharomyces cerevisiae, believed to encode proline oxidase, has been completely sequenced and contains an open reading frame capable of encoding a polypeptide of 476 amino acids in length. The amino terminus of the protein deduced from the DNA sequence has a characteristic mitochondrial import signal; two PUT1-lacZ gene fusions were constructed that produced mitochondrially localized beta-galactosidase in vivo. The transcription initiation and termination sites of the PUT1 mRNA were determined. By using a PUT1-lacZ gene fusion that makes a cytoplasmic beta-galactosidase, the regulation of the PUT1 gene was studied. PUT1 is inducible by proline, responds only slightly to carbon catabolite repression, and is not regulated by the cytochrome activator proteins HAP1 and HAP2. The PUT1 gene is under oxygen regulation; expression in anaerobically grown cells is 10-fold lower than in aerobically grown cells. Oxygen regulation is abolished when cells are respiratory deficient. PUT1 expression in a [rho-] strain grown either aerobically or anaerobically is as high as that seen in a [rho+] strain grown aerobically. Studies on PUT1 promoter deletions define a region between positions -458 and -293 from the translation initiation site that is important for full expression of the PUT1 gene and required for oxygen regulation.
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Mizan, Muhammad Rauful, Desta Wirnas, and Dan Joko Prasetiyono. "Verifikasi Lokus Aluminum Tolerance (Alt) pada Tiga Populasi BC3F1 Padi." Jurnal Agronomi Indonesia (Indonesian Journal of Agronomy) 47, no. 1 (April 30, 2019): 9–17. http://dx.doi.org/10.24831/jai.v47i1.18664.
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Most of marginal lands in Indonesia are in the form of acid dry land with low available P and high Al concentrations. Development of tolerant rice varieties to P deficiency and Al toxicity is one way to increase rice production. This study aimed to select BC3F1-Pup1+Alt genotypes from three crosses based on foreground and background markers. This research was conducted at the Indonesian Center for Agricultural Biotechnology and Genetic Resources Research and Development, Bogor, from August to December 2015. The materials used were 300 genotypes of BC3F1 Dodokan-Pup1+Alt, BC3F1 Situ Bagendit-Pup1+Alt, BC3F1 Batur-Pup1+Alt, and the parents. The research included selection in modified Yoshida’s nutrient solutions (0.5 ppm P dan 60 ppm Al) followed by foreground selection and background selection. Selection using Yoshida’s nutrient solution resulted in 150 genotypes with longer root than the recipient parent in each of the BC3F1 populations. Selection with foreground markers using markers RM1361 and RM12031 produced 85 genotypes of BC3F1 Dodokan-Pup1+Alt (56.6%), 105 genotypes of BC3F1 Situ Bagendit-Pup1+Alt (70%), and 77 genotypes of BC3F1 Batur-Pup1+Alt (51.33%). Selection using background markers revealed that genotype number 116 (BC3F1 Dodokan-Pup1+Alt), number 2 (BC3F1 Situ Bagendit-Pup1+Alt), and number 129 (BC3F1 Batur-Pup1+Alt) were the best genotypes with percentage of parent recovery of 95%, 90%, and 90.5%, respectively. These three genotypes were verified to have Alt loci and had the largest genetic proportion of restoring parents. Keywords: Alt, background markers, foreground markers, Pup1, upland rice
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Saitoh, Atsushi, Yuki Takada, Mayu Horie, and Tomoya Kotani. "Pumilio1 phosphorylation precedes translational activation of its target mRNA in zebrafish oocytes." Zygote 26, no. 5 (October 2018): 372–80. http://dx.doi.org/10.1017/s0967199418000369.
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SummaryTranslational regulation of mRNAs is crucial for promoting various cellular and developmental processes. Pumilio1 (Pum1) has been shown to play key roles in translational regulation of target mRNAs in many systems of diverse organisms. In zebrafish immature oocytes, Pum1 was shown to bind to cyclin B1 mRNA and promote the formation of cyclin B1 RNA granules. This Pum1-mediated RNA granule formation seemed critical to determine the timing of translational activation of cyclin B1 mRNA during oocyte maturation, leading to activation of maturation/M-phase-promoting factor (MPF) at the appropriate timing. Despite its fundamental importance, the mechanisms of translational regulation by Pum1 remain elusive. In this study, we examined the phosphorylation of Pum1 as a first step to understand the mechanisms of Pum1-mediated translation. SDS-PAGE analyses and phosphatase treatments showed that Pum1 was phosphorylated at multiple sites during oocyte maturation. This phosphorylation began in an early period after induction of oocyte maturation, which preceded the polyadenylation of cyclin B1 mRNA. Interestingly, depolymerization of actin filaments in immature oocytes caused phosphorylation of Pum1, disassembly of cyclin B1 RNA granules, and polyadenylation of cyclin B1 mRNA but not translational activation of the mRNA. Overexpression of the Pum1 N-terminus prevented the phosphorylation of Pum1, disassembly of cyclin B1 RNA granules, and translational activation of the mRNA even after induction of oocyte maturation. These results suggest that Pum1 phosphorylation in the early period of oocyte maturation is one of the key processes for promoting the disassembly of cyclin B1 RNA granules and translational activation of target mRNA.
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Wang, S. S., and M. C. Brandriss. "Proline utilization in Saccharomyces cerevisiae: analysis of the cloned PUT1 gene." Molecular and Cellular Biology 6, no. 7 (July 1986): 2638–45. http://dx.doi.org/10.1128/mcb.6.7.2638.
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The PUT1 gene was isolated by functional complementation of a put1 (proline oxidase-deficient) mutation in Saccharomyces cerevisiae. Three independent clones with overlapping inserts of 6.8, 10.5, and 11 kilobases (kb) were isolated from S. cerevisiae genomic libraries in YEp24 (2 micron) and YCp50 (CEN) plasmids. The identity of the PUT1 gene was determined by a gene disruption technique, and Southern hybridization and genetic analyses confirmed that the bona fide gene had been cloned. Plasmids containing the PUT1 gene restored regulated levels of proline oxidase activity to put1 recipient strains. The PUT1 DNA was present in a single copy in the yeast genome and encoded a transcript of ca. 1.5 kb. S1 nuclease protection experiments were used to determine the direction of transcription of the PUT1 message and to localize its 5' and 3' termini within a subcloned 3-kb DNA fragment. Approximately 50-fold more PUT1-specific mRNA was detected in induced (proline-grown) cells than in uninduced (ammonia-grown) cells. A yeast strain carrying the previously identified put3 regulatory mutation that caused constitutive levels of proline oxidase activity was found to have sevenfold elevated PUT1 mRNA levels under noninducing conditions. The absence of a functional electron transport system in vegetative petite (rho-) strains interfered with their ability to use proline as a nitrogen source. Although these strains were Put- and made no detectable proline oxidase activity, PUT1 message was detected under inducing conditions. The PUT1 gene was mapped distal to the GAL2 gene on chromosome XII by tetrad analysis.
8
Wang, S. S., and M. C. Brandriss. "Proline utilization in Saccharomyces cerevisiae: analysis of the cloned PUT1 gene." Molecular and Cellular Biology 6, no. 7 (July 1986): 2638–45. http://dx.doi.org/10.1128/mcb.6.7.2638-2645.1986.
Full textAbstract:
The PUT1 gene was isolated by functional complementation of a put1 (proline oxidase-deficient) mutation in Saccharomyces cerevisiae. Three independent clones with overlapping inserts of 6.8, 10.5, and 11 kilobases (kb) were isolated from S. cerevisiae genomic libraries in YEp24 (2 micron) and YCp50 (CEN) plasmids. The identity of the PUT1 gene was determined by a gene disruption technique, and Southern hybridization and genetic analyses confirmed that the bona fide gene had been cloned. Plasmids containing the PUT1 gene restored regulated levels of proline oxidase activity to put1 recipient strains. The PUT1 DNA was present in a single copy in the yeast genome and encoded a transcript of ca. 1.5 kb. S1 nuclease protection experiments were used to determine the direction of transcription of the PUT1 message and to localize its 5' and 3' termini within a subcloned 3-kb DNA fragment. Approximately 50-fold more PUT1-specific mRNA was detected in induced (proline-grown) cells than in uninduced (ammonia-grown) cells. A yeast strain carrying the previously identified put3 regulatory mutation that caused constitutive levels of proline oxidase activity was found to have sevenfold elevated PUT1 mRNA levels under noninducing conditions. The absence of a functional electron transport system in vegetative petite (rho-) strains interfered with their ability to use proline as a nitrogen source. Although these strains were Put- and made no detectable proline oxidase activity, PUT1 message was detected under inducing conditions. The PUT1 gene was mapped distal to the GAL2 gene on chromosome XII by tetrad analysis.
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Morris, Adam R., Neelanjan Mukherjee, and Jack D. Keene. "Ribonomic Analysis of Human Pum1 Reveals cis-trans Conservation across Species despite Evolution of Diverse mRNA Target Sets." Molecular and Cellular Biology 28, no. 12 (April 14, 2008): 4093–103. http://dx.doi.org/10.1128/mcb.00155-08.
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ABSTRACT PUF family proteins are among the best-characterized regulatory RNA-binding proteins in nonmammalian species, but relatively little is known about mRNA targets or functions of mammalian PUF proteins. In this study, we used ribonomic analysis to identify and analyze mRNAs associated with ribonucleoproteins containing an endogenous human PUF protein, Pum1. Pum1-associated mRNAs were highly enriched for genes encoding proteins that function in transcriptional regulation and cell cycle/proliferation, results consistent with the posttranscriptional RNA regulon model and the proposed ancestral functions of PUF proteins in stem cell biology. Analysis of 3′ untranslated region sequences of Pum1-associated mRNAs revealed a core Pum1 consensus sequence, UGUAHAUA. Pum1 knockdown demonstrated that Pum1 enhances decay of associated mRNAs, and relocalization of Pum1 to stress granules suggested that Pum1 functions in repression of translation. This study is the first in vivo genome-wide mRNA target identification of a mammalian PUF protein and provides direct evidence that human PUF proteins regulate stability of associated mRNAs. Comparison of Pum1-associated mRNAs to mRNA targets of PUF proteins from Saccharomyces cerevisiae and Drosophila melanogaster demonstrates how a well-conserved RNA-binding domain and cognate binding sequence have been evolutionarily rewired to regulate the collective expression of different sets of functionally related genes.
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Hidayatun, Nurul, and Joko Prasetiyono. "Effect of Introgression of Pup1 Locus on Rice Seedling under Phosphorus Deficiency." Jurnal AgroBiogen 14, no. 2 (March 15, 2019): 97. http://dx.doi.org/10.21082/jbio.v14n2.2018.p97-104.
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<p>The lack of soil-phosphorus (P) element will result in plant growth retardation. Plants could survive in P deficiency stress by increasing the ability of P uptake or by increasing the efficiency in the P utilization. The aims of this study were to understand genetic composition of rice genotypes possessing Pup1 locus and to know root and leaf growth responses at different P availability condition. The three rice genotypes (IR74, IR74-Pup1, and Kasalath) were analyzed for their genetic composition using SNP markers. The phenotypic experiment was arranged using a Completely Randomized Design with four replications and performed hydroponically in nutrient solution with different availability of P. The result showed that IR74-Pup1 had 84.4% similarities to its parent (IR74) with 13.6% of donor segments, where the Pup1 locus located. The influence of Pup1 locus<br />introgression on total length, surface area, diameter, and volume of the root varied at each growth stage. IR74 and IR74-Pup1 had root and leaf growth restriction on low P, but Pup1 locus introgression showed better growth performance, both in normal P and in low P conditions. The introgression of Pup1 locus increases plant ability to reduce the impact of growth inhibition<br />caused by P deficiency. </p>
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Apponi, Luciano H., Seth M. Kelly, Michelle T. Harreman, Alexander N. Lehner, Anita H. Corbett, and Sandro R. Valentini. "An Interaction between Two RNA Binding Proteins, Nab2 and Pub1, Links mRNA Processing/Export and mRNA Stability." Molecular and Cellular Biology 27, no. 18 (July 16, 2007): 6569–79. http://dx.doi.org/10.1128/mcb.00881-07.
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ABSTRACT mRNA stability is modulated by elements in the mRNA transcript and their cognate RNA binding proteins. Poly(U) binding protein 1 (Pub1) is a cytoplasmic Saccharomyces cerevisiae mRNA binding protein that stabilizes transcripts containing AU-rich elements (AREs) or stabilizer elements (STEs). In a yeast two-hybrid screen, we identified nuclear poly(A) binding protein 2 (Nab2) as being a Pub1-interacting protein. Nab2 is an essential nucleocytoplasmic shuttling mRNA binding protein that regulates poly(A) tail length and mRNA export. The interaction between Pub1 and Nab2 was confirmed by copurification and in vitro binding assays. The interaction is mediated by the Nab2 zinc finger domain. Analysis of the functional link between these proteins reveals that Nab2, like Pub1, can modulate the stability of specific mRNA transcripts. The half-life of the RPS16B transcript, an ARE-like sequence-containing Pub1 target, is decreased in both nab2-1 and nab2-67 mutants. In contrast, GCN4, an STE-containing Pub1 target, is not affected. Similar results were obtained for other ARE- and STE-containing Pub1 target transcripts. Further analysis reveals that the ARE-like sequence is necessary for Nab2-mediated transcript stabilization. These results suggest that Nab2 functions together with Pub1 to modulate mRNA stability and strengthen a model where nuclear events are coupled to the control of mRNA turnover in the cytoplasm.
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Anderson, J. T., M. R. Paddy, and M. S. Swanson. "PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 10 (October 1993): 6102–13. http://dx.doi.org/10.1128/mcb.13.10.6102.
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Proteins that directly associate with nuclear polyadenylated RNAs, or heterogeneous nuclear RNA-binding proteins (hnRNPs), and those that associate with cytoplasmic mRNAs, or mRNA-binding proteins (mRNPs), play important roles in regulating gene expression at the posttranscriptional level. Previous work with a variety of eukaryotic cells has demonstrated that hnRNPs are localized predominantly within the nucleus whereas mRNPs are cytoplasmic. While studying proteins associated with polyadenylated RNAs in Saccharomyces cerevisiae, we discovered an abundant polyuridylate-binding protein, PUB1, which appears to be both an hnRNP and an mRNP. PUB1 and PAB1, the polyadenylate tail-binding protein, are the two major proteins cross-linked by UV light to polyadenylated RNAs in vivo. The deduced primary structure of PUB1 indicates that it is a member of the ribonucleoprotein consensus sequence family of RNA-binding proteins and is structurally related to the human hnRNP M proteins. Even though the PUB1 protein is a major cellular polyadenylated RNA-binding protein, it is nonessential for cell growth. Indirect cellular immunofluorescence combined with digital image processing allowed a detailed comparison of the intracellular distributions of PUB1 and PAB1. While PAB1 is predominantly, and relatively uniformly, distributed within the cytoplasm, PUB1 is localized in a nonuniform pattern throughout both the nucleus and the cytoplasm. The cytoplasmic distribution of PUB1 is considerably more discontinuous than that of PAB1. Furthermore, sucrose gradient sedimentation analysis demonstrates that PAB1 cofractionates with polyribosomes whereas PUB1 does not. These results suggest that PUB1 is both an hnRNP and an mRNP and that it may be stably bound to a translationally inactive subpopulation of mRNAs within the cytoplasm.
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Anderson, J. T., M. R. Paddy, and M. S. Swanson. "PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 10 (October 1993): 6102–13. http://dx.doi.org/10.1128/mcb.13.10.6102-6113.1993.
Full textAbstract:
Proteins that directly associate with nuclear polyadenylated RNAs, or heterogeneous nuclear RNA-binding proteins (hnRNPs), and those that associate with cytoplasmic mRNAs, or mRNA-binding proteins (mRNPs), play important roles in regulating gene expression at the posttranscriptional level. Previous work with a variety of eukaryotic cells has demonstrated that hnRNPs are localized predominantly within the nucleus whereas mRNPs are cytoplasmic. While studying proteins associated with polyadenylated RNAs in Saccharomyces cerevisiae, we discovered an abundant polyuridylate-binding protein, PUB1, which appears to be both an hnRNP and an mRNP. PUB1 and PAB1, the polyadenylate tail-binding protein, are the two major proteins cross-linked by UV light to polyadenylated RNAs in vivo. The deduced primary structure of PUB1 indicates that it is a member of the ribonucleoprotein consensus sequence family of RNA-binding proteins and is structurally related to the human hnRNP M proteins. Even though the PUB1 protein is a major cellular polyadenylated RNA-binding protein, it is nonessential for cell growth. Indirect cellular immunofluorescence combined with digital image processing allowed a detailed comparison of the intracellular distributions of PUB1 and PAB1. While PAB1 is predominantly, and relatively uniformly, distributed within the cytoplasm, PUB1 is localized in a nonuniform pattern throughout both the nucleus and the cytoplasm. The cytoplasmic distribution of PUB1 is considerably more discontinuous than that of PAB1. Furthermore, sucrose gradient sedimentation analysis demonstrates that PAB1 cofractionates with polyribosomes whereas PUB1 does not. These results suggest that PUB1 is both an hnRNP and an mRNP and that it may be stably bound to a translationally inactive subpopulation of mRNAs within the cytoplasm.
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Uyhazi, Katherine E., Yiying Yang, Na Liu, Hongying Qi, Xiao A. Huang, Winifred Mak, Scott D. Weatherbee, et al. "Pumilio proteins utilize distinct regulatory mechanisms to achieve complementary functions required for pluripotency and embryogenesis." Proceedings of the National Academy of Sciences 117, no. 14 (March 20, 2020): 7851–62. http://dx.doi.org/10.1073/pnas.1916471117.
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Gene regulation in embryonic stem cells (ESCs) has been extensively studied at the epigenetic-transcriptional level, but not at the posttranscriptional level. Pumilio (Pum) proteins are among the few known translational regulators required for stem-cell maintenance in invertebrates and plants. Here we report the essential function of two murine Pum proteins, Pum1 and Pum2, in ESCs and early embryogenesis. Pum1/2 double-mutant ESCs display severely reduced self-renewal and differentiation, and Pum1/2 double-mutant mice are developmentally delayed at the morula stage and lethal by embryonic day 8.5. Remarkably, Pum1-deficient ESCs show increased expression of pluripotency genes but not differentiation genes, whereas Pum2-deficient ESCs show decreased pluripotency markers and accelerated differentiation. Thus, despite their high homology and overlapping target messenger RNAs (mRNAs), Pum1 promotes differentiation while Pum2 promotes self-renewal in ESCs. Pum1 and Pum2 achieve these two complementary aspects of pluripotency by forming a negative interregulatory feedback loop that directly regulates at least 1,486 mRNAs. Pum1 and Pum2 regulate target mRNAs not only by repressing translation, but also by promoting translation and enhancing or reducing mRNA stability of different target mRNAs. Together, these findings reveal distinct roles of individual mammalian Pum proteins in ESCs and their essential functions in ESC pluripotency and embryogenesis.
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Forsburg, S. L., and P. Nurse. "Analysis of the Schizosaccharomyces pombe cyclin puc1: evidence for a role in cell cycle exit." Journal of Cell Science 107, no. 3 (March 1, 1994): 601–13. http://dx.doi.org/10.1242/jcs.107.3.601.
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The puc1+ gene, encoding a G1-type cyclin from the fission yeast Schizosaccharomyces pombe, was originally isolated by complementation in the budding yeast Saccharomyces cerevisiae. Here, we report the molecular characterization of this gene and analyse its role in S. pombe. We fail to identify any function of this cyclin at the mitotic G1/S transition in S. pombe, but demonstrate that it does function in exit from the mitotic cycle. Expression of the puc1+ gene is increased during nitrogen starvation, and puc1 affects the timing of sexual development in response to starvation. Overexpression of the puc1 protein blocks sexual development, and rescues pat1ts cells, which would otherwise undergo a lethal meiosis. We conclude that puc1 contributes to negative regulation of the timing of sexual development in fission yeast, and functions at the transition between cycling and non-cycling cells.
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Buchwald, Ulrike K., Andrew Lees, Michael Steinitz, and Liise-anne Pirofski. "A Peptide Mimotope of Type 8 Pneumococcal Capsular Polysaccharide Induces a Protective Immune Response in Mice." Infection and Immunity 73, no. 1 (January 2005): 325–33. http://dx.doi.org/10.1128/iai.73.1.325-333.2005.
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ABSTRACT Increasing antibiotic resistance and a rising patient population at risk for infection due to impaired immunity underscore the importance of vaccination against pneumococci. However, available capsular polysaccharide vaccines are often poorly immunogenic in patients at risk for pneumococcal disease. The goal of this study was to explore the potential of peptide mimotopes to function as alternative vaccine antigens to elicit a type-specific antibody response to pneumococci. We used a human monoclonal immunoglobulin A (IgA) antibody (NAD) to type 8 Streptococcus pneumoniae capsular polysaccharide (type 8 PS) to screen a phage display library, and the phage PUB1 displaying the peptide FHLPYNHNWFAL was selected after three rounds of biopanning. Inhibition studies with phage-displayed peptide or the peptide PUB1 and type 8 PS showed that PUB1 is a mimetic of type 8 PS. PUB1 conjugated to tetanus toxoid (PUB1-TT) induced a type 8 PS-specific antibody response in BALB/c mice, further defining it as a mimotope of type 8 PS. The administration of immune sera obtained from PUB1-TT-immunized mice earlier (days 14 and 21) and later (days 87 and 100) after primary and reimmunization resulted in a highly significant prolongation of the survival of naive mice after pneumococcal challenge compared to controls. The survival of PUB1-TT-immunized mice was also prolonged after pneumococcal challenge nearly 4 months after primary immunization. The efficacy of PUB1-TT-induced immune sera provides proof of principle that a mimotope-induced antibody response can protect against pneumococci and suggests that peptide mimotopes selected by type-specific human antibodies could hold promise as immunogens for pneumococci.
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Khonsari, Bahar, and Roland Klassen. "Impact of Pus1 Pseudouridine Synthase on Specific Decoding Events in Saccharomyces cerevisiae." Biomolecules 10, no. 5 (May 7, 2020): 729. http://dx.doi.org/10.3390/biom10050729.
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Pus1-dependent pseudouridylation occurs in many tRNAs and at multiple positions, yet the functional impact of this modification is incompletely understood. We analyzed the consequences of PUS1 deletion on the essential decoding of CAG (Gln) codons by tRNAGlnCUG in yeast. Synthetic lethality was observed upon combining the modification defect with destabilized variants of tRNAGlnCUG, pointing to a severe CAG-decoding defect of the hypomodified tRNA. In addition, we demonstrated that misreading of UAG stop codons by a tRNAGlnCUG variant is positively affected by Pus1. Genetic approaches further indicated that mildly elevated temperature decreases the decoding efficiency of CAG and UAG via destabilized tRNAGlnCAG variants. We also determined the misreading of CGC (Arg) codons by tRNAHisGUG, where the CGC decoder tRNAArgICG contains Pus1-dependent pseudouridine, but not the mistranslating tRNAHis. We found that the absence of Pus1 increased CGC misreading by tRNAHis, demonstrating a positive role of the modification in the competition against non-synonymous near-cognate tRNA. Part of the in vivo decoding defects and phenotypes in pus1 mutants and strains carrying destabilized tRNAGlnCAG were suppressible by additional deletion of the rapid tRNA decay (RTD)-relevant MET22, suggesting the involvement of RTD-mediated tRNA destabilization.
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Tasliah, Tasliah, Joko Prasetiyono, Tintin Suhartini, and Ida Hanarida Soemantri. "Ketahanan Galur-Galur Padi Pup1 terhadap Penyakit Blas." Jurnal Penelitian Pertanian Tanaman Pangan 34, no. 1 (April 30, 2015): 29. http://dx.doi.org/10.21082/jpptp.v34n1.2015.p29-36.
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<p>Blast is one of major disease on the upland rice in Indonesia. Upland rice lines derived from Kasalath and NILC443 crosses, containing Pup1 gen locus had been developed and evaluated for P fertilizer efficiency. Those lines would be evaluated for blast resistance, due to the fact that Pup1 locus contains genes involved in plant defend mechanism to disease, including blast disease. The BC2F5 plants derived from six crosses (DK, DN, SK, SN, BK, BN) were used in this research. Responses to blast disease in the green house were evaluated at ICABIOGRAD Bogor from March to April 2011, using combination of three blast races (race 173, 033, and 133). The response to blast disease in the field was evaluated at Taman Bogo Research Station, Lampung, and at farmer’s field in Cikeusal Village, Banten, from January to April 2011. Molecular analysis to trace Pup1 gene locus was conducted at the Molecular Biology Laboratory, using specific primer K20-2, from January to August 2013. Based on the molecular analysis all Pup1 lines showed homozygoes alleles, except the heterozygoes alleles on SK7, SK8, SK15, SK16, BN8 line, which were then not included in the next planting. The responses to blast at greenhouse among lines varied, but the Pup1 lines were mostly at level of moderate resistan (AT). Based on the result from the field experiment, most of Pup1 lines were resistance, however the susceptible check plant (Kencana Bali) did not show blast fungus infection. Differences of the result might be due to the blast testing at the green house which was more favorable for blast fungal growth. The effect of Pup1 gene locus showed clearly on resistance of plants obtained from Situ Bagendit cross, where Situ Bagendit was susceptible and does not contain the Pup1 locus. Additional of Pup1 locus in Situ Bagendit genome had increased the degree of resistant to blast.</p>
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Galez, Henri A., Françoise M. Roelants, Sarah M. Palm, Kendra K. Reynaud, Nicholas T. Ingolia, and Jeremy Thorner. "Phosphorylation of mRNA-Binding Proteins Puf1 and Puf2 by TORC2-Activated Protein Kinase Ypk1 Alleviates Their Repressive Effects." Membranes 11, no. 7 (June 30, 2021): 500. http://dx.doi.org/10.3390/membranes11070500.
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Members of the Puf family of RNA-binding proteins typically associate via their Pumilio homology domain with specific short motifs in the 3’-UTR of an mRNA and thereby influence the stability, localization and/or efficiency of translation of the bound transcript. In our prior unbiased proteome-wide screen for targets of the TORC2-stimulated protein kinase Ypk1, we identified the paralogs Puf1/Jsn1 and Puf2 as high-confidence substrates. Earlier work by others had demonstrated that Puf1 and Puf2 exhibit a marked preference for interaction with mRNAs encoding plasma membrane-associated proteins, consistent with our previous studies documenting that a primary physiological role of TORC2-Ypk1 signaling is maintenance of plasma membrane homeostasis. Here, we show, first, that both Puf1 and Puf2 are authentic Ypk1 substrates both in vitro and in vivo. Fluorescently tagged Puf1 localizes constitutively in cortical puncta closely apposed to the plasma membrane, whereas Puf2 does so in the absence of its Ypk1 phosphorylation, but is dispersed in the cytosol when phosphorylated. We further demonstrate that Ypk1-mediated phosphorylation of Puf1 and Puf2 upregulates production of the protein products of the transcripts to which they bind, with a concomitant increase in the level of the cognate mRNAs. Thus, Ypk1 phosphorylation relieves Puf1- and Puf2-mediated post-transcriptional repression mainly by counteracting their negative effect on transcript stability. Using a heterologous protein-RNA tethering and fluorescent protein reporter assay, the consequence of Ypk1 phosphorylation in vivo was recapitulated for full-length Puf1 and even for N-terminal fragments (residues 1-340 and 143-295) corresponding to the region upstream of its dimerization domain (an RNA-recognition motif fold) encompassing its two Ypk1 phosphorylation sites (both also conserved in Puf2). This latter result suggests that alleviation of Puf1-imposed transcript destabilization does not obligatorily require dissociation of Ypk1-phosphorylated Puf1 from a transcript. Our findings add new insight about how the TORC2-Ypk1 signaling axis regulates the content of plasma membrane-associated proteins to promote maintenance of the integrity of the cell envelope.
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Anderson, Matthew Z., Jeremy Brewer, Upinder Singh, and John C. Boothroyd. "A Pseudouridine Synthase Homologue Is Critical to Cellular Differentiation in Toxoplasma gondii." Eukaryotic Cell 8, no. 3 (March 2009): 398–409. http://dx.doi.org/10.1128/ec.00329-08.
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ABSTRACT Toxoplasma gondii is a haploid protozoan parasite infecting about one in seven people in the United States. Key to the worldwide prevalence of T. gondii is its ability to establish a lifelong, chronic infection by evading the immune system, and central to this is the developmental switch between the two asexual forms, tachyzoites and bradyzoites. A library of mutants defective in tachyzoite-to-bradyzoite differentiation (Tbd−) was created through insertional mutagenesis. This library contains mutants that, compared to the wild type, are between 20% and 74% as efficient at stage conversion. Two mutants, TBD5 and TBD8, with disruptions in a gene encoding a putative pseudouridine synthase, PUS1, were identified. The disruption in TBD8 is in the 5′ end of the PUS1 gene and appears to produce a null allele with a 50% defect in differentiation. This is about the same switch efficiency as obtained with an engineered pus1 deletion mutant (Δpus1). The insertion in TBD5 is within the PUS1 coding region, and this appears to result in a more extreme phenotype of only ∼10% switch efficiency. Complementation of TBD8 with the genomic PUS1 allele restored wild-type differentiation efficiency. Infection of mice with pus1 mutant strains results in increased mortality during the acute phase and higher cyst burdens during the chronic infection, demonstrating an aberrant differentiation phenotype in vivo due to PUS1 disruption. Our results suggest a surprising and important role for RNA modification in this biological process.
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Nishimura, Akira, Yuki Yoshikawa, Kazuki Ichikawa, Tetsuma Takemoto, Ryoya Tanahashi, and Hiroshi Takagi. "Longevity Regulation by Proline Oxidation in Yeast." Microorganisms 9, no. 8 (August 2, 2021): 1650. http://dx.doi.org/10.3390/microorganisms9081650.
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Proline is a pivotal and multifunctional amino acid that is used not only as a nitrogen source but also as a stress protectant and energy source. Therefore, proline metabolism is known to be important in maintaining cellular homeostasis. Here, we discovered that proline oxidation, catalyzed by the proline oxidase Put1, a mitochondrial flavin-dependent enzyme converting proline into ∆1-pyrroline-5-carboxylate, controls the chronological lifespan of the yeast Saccharomyces cerevisiae. Intriguingly, the yeast strain with PUT1 deletion showed a reduced chronological lifespan compared with the wild-type strain. The addition of proline to the culture medium significantly increased the longevity of wild-type cells but not that of PUT1-deleted cells. We next found that induction of the transcriptional factor Put3-dependent PUT1 and degradation of proline occur during the aging of yeast cells. Additionally, the lifespan of the PUT3-deleted strain, which is deficient in PUT1 induction, was shorter than that of the wild-type strain. More importantly, the oxidation of proline by Put1 helped maintain the mitochondrial membrane potential and ATP production through the aging period. These results indicate that mitochondrial energy metabolism is maintained through oxidative degradation of proline and that this process is important in regulating the longevity of yeast cells.
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Sota, Masahiro, Haruhiko Kawasaki, and Masataka Tsuda. "Structure of Haloacetate-Catabolic IncP-1β Plasmid pUO1 and Genetic Mobility of Its Residing Haloacetate-Catabolic Transposon." Journal of Bacteriology 185, no. 22 (November 15, 2003): 6741–45. http://dx.doi.org/10.1128/jb.185.22.6741-6745.2003.
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ABSTRACT The self-transmissible plasmid pUO1 from Delftia acidovorans strain B carries two haloacetate-catabolic transposons, TnHad1 and TnHad2, and the mer genes for resistance to mercury. The complete 67,066-bp sequence of pUO1 revealed that the mer genes were also carried by two Tn402/Tn5053-like transposons, Tn4671 and Tn4672, and that the pUO1 backbone regions shared 99% identity to those of the archetype IncP-1β plasmid R751. Comparison of pUO1 with three other IncP-1β plasmids illustrated the importance of transposon insertion in the diversity and evolution of this group of plasmids. Mutational analysis of the four outermost residues in the inverted repeats (IRs) of TnHad2, a Tn21-related transposon, revealed a crucial role of the second residue of its IRs in transposition.
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Pereira, Ítalo S., Fernanda Z. Barreto, Thiago WA Balsalobre, Fernando C. Sala, Cyro P. Costa, and Monalisa S. Carneiro. "Validação de marcadores moleculares associados à pungência em pimenta." Horticultura Brasileira 33, no. 2 (June 2015): 189–95. http://dx.doi.org/10.1590/s0102-053620150000200009.
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A pungência em frutos de pimenta do gênero Capsicum, devido à presença de capsaicinóides, é uma das características mais atrativas e muito valorizadas pela culinária mundial. Neste trabalho, objetivou-se validar e avaliar a eficiência de predição dos marcadores moleculares pun1¹, pun1³ e o SNP identificado pelo método tetra-primer ARMS-PCR para a determinação de pungência em acessos de Capsicum spp. Trinta e seis acessos do Banco de Germoplasma da Universidade Federal de São Carlos foram avaliados através de análises sensoriais (em frutos maduros) e moleculares para pungência (na fase de plântula através da extração do DNA em folhas). Os marcadores SNP ARMS-PCR, pun1¹ e pun1³ foram usados na avaliação molecular. Os resultados mostram a eficiência desses marcadores para uso de caracterização molecular de acessos de Capsicum ssp. para o caráter pungência.
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Prasetiyono, Joko, and Tasliah Tasliah. "Pemetaan, Karakterisasi, dan Pengembangan Primer-primer Lokus Pup1 (P uptake 1) pada Padi untuk Peningkatan Toleransi terhadap Defisiensi Fosfor." Jurnal AgroBiogen 8, no. 3 (August 15, 2016): 120. http://dx.doi.org/10.21082/jbio.v8n3.2012.p120-129.
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<p>Phosphorus (P) is the second most important nutrient for<br />plants after nitrogen, but is available in very low amount. P<br />deficiency in rice would reduce the number of tillers and<br />grain production. There are numerous publications on<br />exploration of genes that are associated with P. Many<br />researches on P that are directed to breeding program and<br />involving many countries/institutions focus on Pup1<br />research. Pup1 (P uptake 1) is associated with P uptake has<br />been well mapped on chromosome 12 at a distance of 15.31<br />to 15.47 Mb and microsatellite markers between RM28073<br />and RM28102 can be used as a selection tool in the MAB<br />(Marker Assisted Backrossing) program. Indonesia is very<br />concerned with this research because of P-deficient<br />problem. This review aims to provide current information of<br />research that explore the genes in Pup1 locus. This review<br />outlines the history of Pup1 mapping, to explain sequence<br />and expression analysis of Pup1, and to inform of Pup1<br />specific primers. The latest information is expected to be<br />useful for rice breeders in Indonesia, especially for those<br />who are interested to P deficiency research. Study of genes<br />within Pup1 locus is still ongoing, and found that some<br />genes do not contribute directly to P uptake. This may<br />indicate that Pup1 locus use other mechanisms in the P<br />uptake. This may indicate that some genes (dirigent-like,<br />fatty acid α-dioxygenase, aspartic proteinases) play a role in<br />the increasing level of lignin in P deficient condition.<br />Increasing level of lignin would increase the volume of roots<br />and thus increasing P uptake and resistance to biotic and<br />abiotic stresses. Specific markers to detect the genes in the<br />Pup1 locus have been successfully developed, and can be<br />used for breeding and exploration activities on Indonesian<br />rice germplasm.</p>
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Liu, Yonghong, Linlin Qu, Yuanyuan Liu, Bernard Roizman, and Grace Guoying Zhou. "PUM1 is a biphasic negative regulator of innate immunity genes by suppressing LGP2." Proceedings of the National Academy of Sciences 114, no. 33 (July 31, 2017): E6902—E6911. http://dx.doi.org/10.1073/pnas.1708713114.
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PUM1 is an RNA binding protein shown to regulate the stability and function of mRNAs bearing a specific sequence. We report the following: (i) A key function of PUM1 is that of a repressor of key innate immunity genes by repressing the expression of LGP2. Thus, between 12 and 48 hours after transfection of human cells with siPUM1 RNA there was an initial (phase 1) upsurge of transcripts encoding LGP2, CXCL10, IL6, and PKR. This was followed 24 hours later (phase 2) by a significant accumulation of mRNAs encoding RIG-I, SP100, MDA5, IFIT1, PML, STING, and IFNβ. The genes that were not activated encoded HDAC4 and NF-κB1. (ii) Simultaneous depletion of PUM1 and LGP2, CXCL10, or IL6 revealed that up-regulation of phase 1 and phase 2 genes was the consequence of up-regulation of LGP2. (iii) IFNβ produced 48–72 hours after transfection of siPUM1 was effective in up-regulating LGP2 and phase 2 genes and reducing the replication of HSV-1 in untreated cells. (iv) Because only half of genes up-regulated in phase 1 and 2 encode mRNAs containing PUM1 binding sites, the upsurge in gene expression could not be attributed solely to stabilization of mRNAs in the absence of PUM1. (v) Lastly, depletion of PUM2 does not result in up-regulation of phase 1 or phase 2 genes. The results of the studies presented here indicate that PUM1 is a negative regulator of LGP2, a master regulator of innate immunity genes expressed in a cascade fashion.
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Takei, Natsumi, Yuki Takada, Shohei Kawamura, Keisuke Sato, Atsushi Saitoh, Jenny Bormann, Wai Shan Yuen, John Carroll, and Tomoya Kotani. "Changes in subcellular structures and states of pumilio 1 regulate the translation of target Mad2 and cyclin B1 mRNAs." Journal of Cell Science 133, no. 23 (November 4, 2020): jcs249128. http://dx.doi.org/10.1242/jcs.249128.
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ABSTRACTTemporal and spatial control of mRNA translation has emerged as a major mechanism for promoting diverse biological processes. However, the molecular nature of temporal and spatial control of translation remains unclear. In oocytes, many mRNAs are deposited as a translationally repressed form and are translated at appropriate times to promote the progression of meiosis and development. Here, we show that changes in subcellular structures and states of the RNA-binding protein pumilio 1 (Pum1) regulate the translation of target mRNAs and progression of oocyte maturation. Pum1 was shown to bind to Mad2 (also known as Mad2l1) and cyclin B1 mRNAs, assemble highly clustered aggregates, and surround Mad2 and cyclin B1 RNA granules in mouse oocytes. These Pum1 aggregates were dissolved prior to the translational activation of target mRNAs, possibly through phosphorylation. Stabilization of Pum1 aggregates prevented the translational activation of target mRNAs and progression of oocyte maturation. Together, our results provide an aggregation-dissolution model for the temporal and spatial control of translation.
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Tasliah, Tasliah, Ma'sumah Ma'sumah, and Joko Prasetiyono. "Eksplorasi Lokus Pup1 Berbasis Marka Molekuler pada 55 Genotipe Padi." Jurnal AgroBiogen 12, no. 2 (February 13, 2018): 63. http://dx.doi.org/10.21082/jbio.v12n2.2016.p63-72.
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<p>Fosfor (P) adalah unsur penting pada padi yang ketersediaan di bumi semakin berkurang. Genotipe yang mudah menangkap P dan efisien dalam menggunakan P sangat membantu mengatasi defisiensi P. Kasalath sebagai genotipe dari luar Indonesia saat ini terbukti memiliki lokus <em>Pup1</em> yang memiliki kemampuan menangkap dan menggunakan P secara efisien. Eksplorasi lokus <em>Pup1</em> pada plasma nutfah padi Indonesia diharapkan bisa memperoleh genotipe baru yang memiliki lokus <em>Pup1</em>. Penelitian ini bertujuan untuk mengeksplorasi 55 genotipe padi, baik padi sawah maupun padi gogo dengan menggunakan marka-marka spesifik gen-gen yang berada di dalam lokus <em>Pup1</em>. Penelitian dilakukan di Laboratorium Biologi Molekuler, Balai Besar Bioteknologi dan Sumber Daya Genetik Pertanian pada bulan Januari sd Desember 2015. Genotipe padi yang digunakan berjumlah 55 genotipe, terdiri dari 3 genotipe cek (Kasalath, NIL-C443, dan Nipponbare), 52 genotipe padi Indonesia terdiri dari 37 padi gogo dan 15 padi sawah. Marka yang digunakan adalah empat marka yang spesifik berada di dalam lokus <em>Pup1</em>, yakni K05, K20−2 + <em>Bsp12861</em>, K29−1, dan K46−2. Lima genotipe (Kasalath, NIL-C443, Gajah Mungkur, Cabacu, dan IR36) yang memiliki alel Kasalath pada keempat marka disekuen pada pita yang dihasilkan oleh marka K20−2 + <em>Bsp12861</em> dan K46−2, yang menghasilkan protein dirigen dan protein serin/treonin. Analisis kesamaan sekuen dilakukan menggunakan beberapa perangkat lunak yang ada di dalam program <em>DNA Star Lasergen</em> 11 <em>Core Suite</em>. Sekuen genotipe Kasalath, NIL-C443, Gajah Mungkur, Cabacu, dan IR36 daerah marka K20−2 + <em>Bsp12681</em> dan K46−2 memiliki kesamaan yang bervariasi (54,7−95,2% dan 94,6−97,5%) dibanding dengan sekuen <em>Pup1 </em>rujukan. Genotipe Gajah Mungkur, Cabacu, dan IR36 memiliki potensi sebagai sumber lokus <em>Pup1</em> yang baru menggantikan Kasalath.</p>
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Aftab, rA, A. H. Khan, A. S. Adnan, S. A. Syed Sulaiman, tM Khan, and tH Malhi. "PUK1 - DR RAJA AHSAN AFTAB." Value in Health 21 (October 2018): S475. http://dx.doi.org/10.1016/j.jval.2018.09.2799.
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Chankaew, Sompong, Tidarat Monkham, Wanwipa Pinta, Jirawat Sanitchon, Wanwipa Kaewpradit, and Peerasak Srinives. "Screening Tolerance to Phosphorus Deficiency and Validation of Phosphorus Uptake 1 (Pup1) Gene-Linked Markers in Thai Indigenous Upland Rice Germplasm." Agronomy 9, no. 2 (February 12, 2019): 81. http://dx.doi.org/10.3390/agronomy9020081.
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Phosphorus (P) deficiency is a major factor limiting rice yield throughout the world. Fortunately, some rice accessions are tolerant and can thrive well, even in soils with low P content. The ability to uptake P is heritable, and thus can be incorporated into rice cultivars through standard breeding methods. The objective of this study was to screen for tolerance to phosphorus deficiency and validate the tolerant accessions with phosphorus uptake 1 (Pup1) gene-linked markers in Thai indigenous upland rice germplasm. One hundred sixty-eight rice varieties were screened in a solution culture and assigned a phosphorus deficiency tolerance index and plant symptom score. Eleven upland rice accessions (ULR026, ULR031, ULR124, ULR145, ULR180, ULR183, ULR185, ULR186, ULR213, ULR260, and ULR305), together with the lowland rice cultivar (PLD), were classified as tolerant. They were each validated by nine markers linked to the Pup1 locus and observed for the expected polymerase chain reaction (PCR) product of 0 to 9 markers. The presence or absence of the tolerant allele at the Pup1 locus showed only a slight relationship with the tolerance. Moreover, some lines such as ULR183 and ULR213 expressed high tolerance without the Pup1-linked gene product. Both accessions are useful for the exploration of novel genes conferring tolerance to phosphorus deficiency.
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Smialek, Maciej J., Erkut Ilaslan, Marcin P. Sajek, Aleksandra Swiercz, Damian M. Janecki, Kamila Kusz-Zamelczyk, Tomasz Wozniak, et al. "Characterization of RNP Networks of PUM1 and PUM2 Post-Transcriptional Regulators in TCam-2 Cells, a Human Male Germ Cell Model." Cells 9, no. 4 (April 16, 2020): 984. http://dx.doi.org/10.3390/cells9040984.
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Mammalian Pumilio (PUM) proteins are sequence-specific, RNA-binding proteins (RBPs) with wide-ranging roles. They are involved in germ cell development, which has functional implications in development and fertility. Although human PUM1 and PUM2 are closely related to each other and recognize the same RNA binding motif, there is some evidence for functional diversity. To address that problem, first we used RIP-Seq and RNA-Seq approaches, and identified mRNA pools regulated by PUM1 and PUM2 proteins in the TCam-2 cell line, a human male germ cell model. Second, applying global mass spectrometry-based profiling, we identified distinct PUM1- and PUM2-interacting putative protein cofactors, most of them involved in RNA processing. Third, combinatorial analysis of RIP and RNA-Seq, mass spectrometry, and RNA motif enrichment analysis revealed that PUM1 and PUM2 form partially varied RNP-regulatory networks (RNA regulons), which indicate different roles in human reproduction and testicular tumorigenesis. Altogether, this work proposes that protein paralogues with very similar and evolutionary highly conserved functional domains may play divergent roles in the cell by combining with different sets of protein cofactors. Our findings highlight the versatility of PUM paralogue-based post-transcriptional regulation, offering insight into the mechanisms underlying their diverse biological roles and diseases resulting from their dysfunction.
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Khasna, Elhah Nailul, Shelly Zairina, Ria Reinnata Juliandari, Eko Sri Sulasmi, and Dwi Listyorini. "Pun1 Gene Isolation from Capsicum frutescens L. cv Cakra Hijau." KnE Life Sciences 3, no. 4 (March 27, 2017): 70. http://dx.doi.org/10.18502/kls.v3i4.689.
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<p class="Els-Abstract-text"><em>Capsicum frutescens </em>L. is one of chili peppers with high pungency. <em>Capsicum frutescens </em>has several cultivars, one of those is <em>C. frutescens</em> cv. Cakra Hijau. This cultivars is known resistance to pests and diseases as well. Pungency is due to the accumulation of capsaicinoids. <em>Pun1</em> is an important gene responsible for pungency. The full-leght genomic sequence of <em>Pun1</em> is 1897 bp, containing two exons of 738 bp and 590 bpand one intron of 348 bp in between. This study was aimed to isolate <em>Pun1 </em>gene that free from intron. mRNA was isolated with TriReagentâ furthermore RT-PCR method used Qiagent One-Step RT-PCR and two pairs of primer : F1/R1 (F15’-ATG-GCT-TTT-GCA-TTA-CCA-TCA-3’ / R15’- CTT-AGC-TCG-AAG-TGC-ATC-TA-3’) and F2/R2 (F25’-GAA-GGT-GGC-AGA-AGA-ATC-AG-3’/R25’-TTA-GGC-AAT-GAA-CTC-AAG-GA-3’). The result of this study are isolated 738 bp exon-1 and 590 bp exon 2 of <em>Pun1 </em>gene.</p><div><p class="Els-keywords"><em> </em></p><p class="Els-keywords"><strong>Keywords:</strong> Capsaicin;<em> Capsicum frutescens </em>L. cv. Cakra Hijau; exon; <em>Pun1 </em>gene </p></div>
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Juliandri, Ria Reinnata, Shelly Zairina, Elhah Nailul Khasna, Dahlia ., and Dwi Listyorini. "Isolation 3’-end Fragment of Pun1 gene from Capsicum frutescens L. cultivar Cakra Hijau." KnE Life Sciences 3, no. 4 (March 27, 2017): 194. http://dx.doi.org/10.18502/kls.v3i4.704.
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<p><em>Pun1 </em>gene <a href="file:///C:/Users/Mohamad%20Mostafa/Desktop/Knowledge%20E/In%20Press%20Conferences/ICBS-2015/Source%20files/ICBS-2015/Soure%20papers-ICBS-2015/25.%20Ria%20Reinnata-080117_Roy.doc#_msocom_1">[A1]</a> is the one of candidate gene that responsible to determine pungency in Capsicum. In previous researches, 1 310 bp fragment of 1 671 bp <em>Pun1 </em>gene from<em> Capsicum frutescens </em>L. cv. Cakra Hijau had been isolated. The purpose of this research was to isolate of 3’-<em>end</em> fragment and get full length of <em>Pun1</em> gene from <em>C. frutescens</em> L. cv. Cakra Hijau. DNA isolation was done using modified procedure. The method used to isolate the gene was PCR with a pair of primer, <em>forward primer </em>5’-GAA-GGT-GGC-AGA-AGA-ATC-AG-3’ and <em>reverse primer</em> 5’-TTG- TTG ACC-GTA-AAC-TTC-CG- 3’. The result successfully to get 715 bp length DNA fragment. The assembly of this fragment into previous research produced a full length of 1 671 bp <em>Pun1</em> gene from <em>C. frutescens</em> L. cv. Cakra Hijau consist of 738 bp first exon fragment, 348 bp intron fragment, and 585 bp second exon fragment.</p><p class="Els-Abstract-text"> </p><div><p class="Els-keywords"><strong>Keywords:</strong> C. frustescens L. cv. Cakra Hijau; gene isolation; <em>Pun1</em> gene.</p></div>
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PAME, ANNY RUTH, CHRISTINE KREYE, DAVID JOHNSON, SIGRID HEUER, and MATHIAS BECKER. "EFFECTS OF GENOTYPE, SEED P CONCENTRATION AND SEED PRIMING ON SEEDLING VIGOR OF RICE." Experimental Agriculture 51, no. 3 (January 9, 2015): 370–81. http://dx.doi.org/10.1017/s0014479714000362.
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SUMMARYSeedling vigor is important to help ensure good crop establishment. In direct-seeded rice, this is particularly relevant when soil conditions are marginal. In Asia, about one third of the area of rainfed rice is situated on unfavorable soils, many of which are low in plant available P. In such environments, as farmers tend to have few resources, options to overcome poor crop establishment should be low cost and preferably seed-based. The P content of seed depends on genotype and can be augmented by soaking seeds in a P-containing solution prior to seeding (P-priming). In addition, the presence of the Pup1 quantitative trait locus can reportedly confer tolerance to low soil P availability. We tested combinations of seed priming (unprimed control, water priming, P-priming), and inherent seed P concentrations in contrasting rice genotypes (DJ123, Sadri Tor Misri), and two near isogenic sister lines of IR74 with (+Pup1) and without (−Pup1) the Pup1 QTL. Treatment effects on germination were studied in Petri dishes, while seedling growth and P accumulation were assessed using pots with P deficient soil. Germination was less than 75% in seeds with low seed P content. Seed priming with both water and P enhanced germination and seedling growth. In plants growing from high P seeds, water priming outperformed P-priming. In Sadri Tor Misri with low seed P, we observed a tendency for better performance in some parameters when P-primed. While the presence of the Pup1 QTL in IR74 increased shoot biomass and total root length, these effects could be further enhanced by water priming. Combining genetic and seed management approaches may contribute to improved rice establishment in P deficient soils but its effectiveness depends on genotype and seed attributes.
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Urakov, Valery, Olga Mitkevich, Alexander Dergalev, and Michael Ter-Avanesyan. "The Pub1 and Upf1 Proteins Act in Concert to Protect Yeast from Toxicity of the [PSI+] Prion." International Journal of Molecular Sciences 19, no. 11 (November 20, 2018): 3663. http://dx.doi.org/10.3390/ijms19113663.
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The [PSI+] nonsense-suppressor determinant of Saccharomyces cerevisiae is based on the formation of heritable amyloids of the Sup35 (eRF3) translation termination factor. [PSI+] amyloids have variants differing in amyloid structure and in the strength of the suppressor phenotype. The appearance of [PSI+], its propagation and manifestation depend primarily on chaperones. Besides chaperones, the Upf1/2/3, Siw14 and Arg82 proteins restrict [PSI+] formation, while Sla2 can prevent [PSI+] toxicity. Here, we identify two more non-chaperone proteins involved in [PSI+] detoxification. We show that simultaneous lack of the Pub1 and Upf1 proteins is lethal to cells harboring [PSI+] variants with a strong, but not with a weak, suppressor phenotype. This lethality is caused by excessive depletion of the Sup45 (eRF1) termination factor due to its sequestration into Sup35 polymers. We also show that Pub1 acts to restrict excessive Sup35 prion polymerization, while Upf1 interferes with Sup45 binding to Sup35 polymers. These data allow consideration of the Pub1 and Upf1 proteins as a novel [PSI+] detoxification system.
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Andersson, M. Gunnar, and Lage Cerenius. "Pumilio Homologue from Saprolegnia parasitica Specifically Expressed in Undifferentiated Spore Cysts." Eukaryotic Cell 1, no. 1 (February 2002): 105–11. http://dx.doi.org/10.1128/ec.1.1.105-111.2002.
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ABSTRACT The expression of spore-specific marker transcripts at different stages of the asexual life cycle of Saprolegnia parasitica was analyzed. One of the markers, designated puf1, was found to be expressed transiently upon each of several cycles of zoospore encystment and reemergence. The transcript is induced immediately upon zoospore encystment and is rapidly lost when a cyst is triggered to germinate. In nongerminating cysts, puf1 is maintained until a time point when the cysts can no longer be triggered to germinate and thus have become determined for zoospore reemergence. The results show that the cyst stage has two phases, of about equal duration, which are physiologically and transcriptionally distinct and that the transcriptional machinery of oomycetes is also active in nongerminating spores. puf1 encodes a putative mRNA binding protein belonging to a conserved class of proteins including the Drosophila melanogaster Pumilio protein, Caenorhabditis elegans FBF, and Saccharomyces cerevisiae Puf5, all of which are involved in regulation of gene expression by posttranscriptional mechanisms.
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Caligiuri, M., T. Connolly, and D. Beach. "Ran1 functions to control the Cdc10/Sct1 complex through Puc1." Molecular Biology of the Cell 8, no. 6 (June 1997): 1117–28. http://dx.doi.org/10.1091/mbc.8.6.1117.
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We have undertaken a biochemical analysis of the regulation of the G1/S-phase transition and commitment to the cell cycle in the fission yeast Schizosaccharomyces pombe. The execution of Start requires the activity of the Cdc2 protein kinase and the Sct1/Cdc10 transcription complex. Progression through G1 also requires the Ran1 protein kinase whose inactivation leads to activation of the meiotic pathway under conditions normally inhibitory to this process. We have found that in addition to Cdc2, Sct1/Cdc10 complex formation requires Ran1. We demonstrate that the Puc1 cyclin associates with Ran1 and Cdc10 in vivo and that the Ran1 protein kinase functions to control the association between Puc1 and Cdc10. In addition, we present evidence that the phosphorylation state of Cdc10 is altered upon inactivation of Ran1. These results provide biochemical evidence that demonstrate one mechanism by which the Ran1 protein kinase serves to control cell fate through Cdc10 and Puc1.
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Moisseyev, S. "PUP1: PHARMACOECONOMICS IN RUSSIA: FIRST STEPS." Value in Health 2, no. 3 (May 1999): 223–24. http://dx.doi.org/10.1016/s1098-3015(11)71069-5.
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Luu, Van-Duc, Stefanie Brems, Jörg D. Hoheisel, Richard Burchmore, D. Lys Guilbride, and Christine Clayton. "Functional analysis of Trypanosoma brucei PUF1." Molecular and Biochemical Parasitology 150, no. 2 (December 2006): 340–49. http://dx.doi.org/10.1016/j.molbiopara.2006.09.007.
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Su, Wan-Chun, and Paul M. Harrison. "Deep conservation of prion-like composition in the eukaryotic prion-former Pub1/Tia1 family and its relatives." PeerJ 8 (April 17, 2020): e9023. http://dx.doi.org/10.7717/peerj.9023.
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Pub1 protein is an important RNA-binding protein functional in stress granule assembly in budding yeast Saccharomyces cerevisiae and, as its co-ortholog Tia1, in humans. It is unique among proteins in evidencing prion-like aggregation in both its yeast and human forms. Previously, we noted that Pub1/Tia1 was the only protein linked to human disease that has prion-like character and and has demonstrated such aggregation in both species. Thus, we were motivated to probe further into the evolution of the Pub1/Tia1 family (and its close relative Nam8 and its orthologs) to gain a picture of how such a protein has evolved over deep evolutionary time since the last common ancestor of eukaryotes. Here, we discover that the prion-like composition of this protein family is deeply conserved across eukaryotes, as is the prion-like composition of its close relative Nam8/Ngr1. A sizeable minority of protein orthologs have multiple prion-like domains within their sequences (6–20% depending on criteria). The number of RNA-binding RRM domains is conserved at three copies over >86% of the Pub1 family (>71% of the Nam8 family), but proteins with just one or two RRM domains occur frequently in some clades, indicating that these are not due to annotation errors. Overall, our results indicate that a basic scaffold comprising three RNA-binding domains and at least one prion-like region has been largely conserved since the last common ancestor of eukaryotes, providing further evidence that prion-like aggregation may be a very ancient and conserved phenomenon for certain specific proteins.
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Siddiqui, A. H., and M. C. Brandriss. "The Saccharomyces cerevisiae PUT3 activator protein associates with proline-specific upstream activation sequences." Molecular and Cellular Biology 9, no. 11 (November 1989): 4706–12. http://dx.doi.org/10.1128/mcb.9.11.4706.
Full textAbstract:
The PUT1 and PUT2 genes encoding the enzymes of the proline utilization pathway of Saccharomyces cerevisiae are induced by proline and activated by the product of the PUT3 gene. Two upstream activation sequences (UASs) in the PUT1 promoter were identified by homology to the PUT2 UAS. Deletion analysis of the two PUT1 UASs showed that they were functionally independent and additive in producing maximal levels of gene expression. The consensus PUT UAS is a 21-base-pair partially palindromic sequence required in vivo for induction of both genes. The results of a gel mobility shift assay demonstrated that the proline-specific UAS is the binding site of a protein factor. In vitro complex formation was observed in crude extracts of yeast strains carrying either a single genomic copy of the PUT3 gene or the cloned PUT3 gene on a 2 microns plasmid, and the binding was dosage dependent. DNA-binding activity was not observed in extracts of strains carrying either a put3 mutation that caused a noninducible (Put-) phenotype or a deletion of the gene. Wild-type levels of complex formation were observed in an extract of a strain carrying an allele of PUT3 that resulted in a constitutive (Put+) phenotype. Extracts from a strain carrying a PUT3-lacZ gene fusion formed two complexes of slower mobility than the wild-type complex. We conclude that the PUT3 product is either a DNA-binding protein or part of a DNA-binding complex that recognizes the UASs of both PUT1 and PUT2. Binding was observed in extracts of a strain grown in the presence or absence of proline, demonstrating the constitutive nature of the DNA-protein interaction.
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Matunis, M. J., E. L. Matunis, and G. Dreyfuss. "PUB1: a major yeast poly(A)+ RNA-binding protein." Molecular and Cellular Biology 13, no. 10 (October 1993): 6114–23. http://dx.doi.org/10.1128/mcb.13.10.6114.
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The expression of RNA polymerase II transcripts can be regulated at the posttranscriptional level by RNA-binding proteins. Although extensively characterized in metazoans, relatively few RNA-binding proteins have been characterized in the yeast Saccharomyces cerevisiae. Three major proteins are cross-linked by UV light to poly(A)+ RNA in living S. cerevisiae cells. These are the 72-kDa poly(A)-binding protein and proteins of 60 and 50 kDa (S.A. Adam, T.Y. Nakagawa, M.S. Swanson, T. Woodruff, and G. Dreyfuss, Mol. Cell. Biol. 6:2932-2943, 1986). Here, we describe the 60-kDa protein, one of the major poly(A)+ RNA-binding proteins in S. cerevisiae. This protein, PUB1 [for poly(U)-binding protein 1], was purified by affinity chromatography on immobilized poly(rU), and specific monoclonal antibodies to it were produced. UV cross-linking demonstrated that PUB1 is bound to poly(A)+ RNA (mRNA or pre-mRNA) in living cells, and it was detected primarily in the cytoplasm by indirect immunofluorescence. The gene for PUB1 was cloned and sequenced, and the sequence was found to predict a 51-kDa protein with three ribonucleoprotein consensus RNA-binding domains and three glutamine- and asparagine-rich auxiliary domains. This overall structure is remarkably similar to the structures of the Drosophila melanogaster elav gene product, the human neuronal antigen HuD, and the cytolytic lymphocyte protein TIA-1. Each of these proteins has an important role in development and differentiation, potentially by affecting RNA processing. PUB1 was found to be nonessential in S. cerevisiae by gene replacement; however, further genetic analysis should reveal important features of this class of RNA-binding proteins.
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Matunis, M. J., E. L. Matunis, and G. Dreyfuss. "PUB1: a major yeast poly(A)+ RNA-binding protein." Molecular and Cellular Biology 13, no. 10 (October 1993): 6114–23. http://dx.doi.org/10.1128/mcb.13.10.6114-6123.1993.
Full textAbstract:
The expression of RNA polymerase II transcripts can be regulated at the posttranscriptional level by RNA-binding proteins. Although extensively characterized in metazoans, relatively few RNA-binding proteins have been characterized in the yeast Saccharomyces cerevisiae. Three major proteins are cross-linked by UV light to poly(A)+ RNA in living S. cerevisiae cells. These are the 72-kDa poly(A)-binding protein and proteins of 60 and 50 kDa (S.A. Adam, T.Y. Nakagawa, M.S. Swanson, T. Woodruff, and G. Dreyfuss, Mol. Cell. Biol. 6:2932-2943, 1986). Here, we describe the 60-kDa protein, one of the major poly(A)+ RNA-binding proteins in S. cerevisiae. This protein, PUB1 [for poly(U)-binding protein 1], was purified by affinity chromatography on immobilized poly(rU), and specific monoclonal antibodies to it were produced. UV cross-linking demonstrated that PUB1 is bound to poly(A)+ RNA (mRNA or pre-mRNA) in living cells, and it was detected primarily in the cytoplasm by indirect immunofluorescence. The gene for PUB1 was cloned and sequenced, and the sequence was found to predict a 51-kDa protein with three ribonucleoprotein consensus RNA-binding domains and three glutamine- and asparagine-rich auxiliary domains. This overall structure is remarkably similar to the structures of the Drosophila melanogaster elav gene product, the human neuronal antigen HuD, and the cytolytic lymphocyte protein TIA-1. Each of these proteins has an important role in development and differentiation, potentially by affecting RNA processing. PUB1 was found to be nonessential in S. cerevisiae by gene replacement; however, further genetic analysis should reveal important features of this class of RNA-binding proteins.
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Siddiqui, A. H., and M. C. Brandriss. "The Saccharomyces cerevisiae PUT3 activator protein associates with proline-specific upstream activation sequences." Molecular and Cellular Biology 9, no. 11 (November 1989): 4706–12. http://dx.doi.org/10.1128/mcb.9.11.4706-4712.1989.
Full textAbstract:
The PUT1 and PUT2 genes encoding the enzymes of the proline utilization pathway of Saccharomyces cerevisiae are induced by proline and activated by the product of the PUT3 gene. Two upstream activation sequences (UASs) in the PUT1 promoter were identified by homology to the PUT2 UAS. Deletion analysis of the two PUT1 UASs showed that they were functionally independent and additive in producing maximal levels of gene expression. The consensus PUT UAS is a 21-base-pair partially palindromic sequence required in vivo for induction of both genes. The results of a gel mobility shift assay demonstrated that the proline-specific UAS is the binding site of a protein factor. In vitro complex formation was observed in crude extracts of yeast strains carrying either a single genomic copy of the PUT3 gene or the cloned PUT3 gene on a 2 microns plasmid, and the binding was dosage dependent. DNA-binding activity was not observed in extracts of strains carrying either a put3 mutation that caused a noninducible (Put-) phenotype or a deletion of the gene. Wild-type levels of complex formation were observed in an extract of a strain carrying an allele of PUT3 that resulted in a constitutive (Put+) phenotype. Extracts from a strain carrying a PUT3-lacZ gene fusion formed two complexes of slower mobility than the wild-type complex. We conclude that the PUT3 product is either a DNA-binding protein or part of a DNA-binding complex that recognizes the UASs of both PUT1 and PUT2. Binding was observed in extracts of a strain grown in the presence or absence of proline, demonstrating the constitutive nature of the DNA-protein interaction.
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Lin, Kaibo, Shikun Zhang, Qinghua Shi, Mengyi Zhu, Liuze Gao, Wenjuan Xia, Baobao Geng, Zimeng Zheng, and Eugene Yujun Xu. "Essential requirement of mammalian Pumilio family in embryonic development." Molecular Biology of the Cell 29, no. 24 (November 26, 2018): 2922–32. http://dx.doi.org/10.1091/mbc.e18-06-0369.
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Mouse PUMILIO1 (PUM1) and PUMILIO2 (PUM2) belong to the PUF (Pumilio/FBF) family, a highly conserved RNA binding protein family whose homologues play critical roles in embryonic development and germ line stem cell maintenance in invertebrates. However, their roles in mammalian embryonic development and stem cell maintenance remained largely uncharacterized. Here we report an essential requirement of the Pum gene family in early embryonic development. A loss of both Pum1 and Pum2 genes led to gastrulation failure, resulting in embryo lethality at E8.5. Pum-deficient blastocysts, however, appeared morphologically normal, from which embryonic stem cells (ESCs) could be established. Both mutant ESCs and embryos exhibited reduced growth and increased expression of endoderm markers Gata6 and Lama1, making defects in growth and differentiation the likely causes of gastrulation failure. Furthermore, ESC Gata6 transcripts could be pulled down via PUM1 immunoprecipitation and mutation of conserved PUM-binding element on 3′UTR (untranslated region) of Gata6 enhanced the expression of luciferase reporter, implicating PUM-mediated posttranscriptional regulation of Gata6 expression in stem cell development and cell lineage determination. Hence, like its invertebrate homologues, mouse PUM proteins are conserved posttranscriptional regulators essential for embryonic and stem cell development.
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Zheng, Wuxi. "Negation in Longxi Qiang." Language and Linguistics / 語言暨語言學 20, no. 4 (September 24, 2019): 660–94. http://dx.doi.org/10.1075/lali.00053.zhe.
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Abstract Negation in Longxi Qiang shows distinctive features in comparison to other recorded Qiang varieties. The choice between the two negative prefixes /mí-/ and /mì-/ and the volition indicated by these two negative markers in Longxi Qiang are similar to those of negators pu31 and mei55 in Wenchuan Mandarin. To a large extent, pu31 corresponds to /mí-/ and mei55 corresponds to /mì-/. Moreover, two negative constructions with positive meaning in Wenchuan Mandarin are borrowed into Longxi Qiang. I believe that the development of a negation system similar to Wenchuan Mandarin in Longxi Qiang is not a coincidence; language contact is an important factor accounting for it.
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Boening, AJ, MM Chapman, RH Brown, PG Zager, and KB Meyer. "PUR1: HEALTH STATUS OF ELDERLY DIALYSIS PATIENTS." Value in Health 4, no. 2 (September 2001): 162. http://dx.doi.org/10.1046/j.1524-4733.2001.40202-245.x.
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Zairina, Shelly, Elhah Nailul Khasna, Ria Reinnata Juliandari, Eko Sri Sulasmi, and Dwi Listyorini. "Synthesis of cDNA Pun1 gene from Capsicum frutescens L. cv. Cakra Hijau." KnE Life Sciences 3, no. 4 (March 27, 2017): 226. http://dx.doi.org/10.18502/kls.v3i4.709.
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<p class="Els-Abstract-text"><em>Capsicum frutescens</em> L. cv. Cakra Hijau is a local cultivar that has been widely cultivated in Indonesia due to the pungency. Pungent on <em>Capsicum</em> is generated by capsaicin compound encoded by <em>Pun1</em> gene. The sequences of <em>Pun1 </em>gene containing with two exons that located on the upstream and downstream, which are separated by introns in the middle. This study aimed to synthesis of cDNA of <em>Pun1</em> gene from isolated total mRNA using two primers: F1/R1 (<strong><em>F1 </em></strong>5’- ATG GCT TTT GCA TTA CCA TCA -3’; and <strong><em>R1 </em></strong>5’-CTT AGC TCG AAG TGC ATC TA-3’) to synthesis the exon-1 sequences and F2/R2 (<strong><em>F2 </em></strong>5’-GAA GGT GGC AGA AGA ATC AG-3’; and <strong><em>R2 </em></strong>5’-TTA GGC AAT GAA CTC AAG GA-3’) to synthesis the exon-2 sequences. The cDNAs resulted from RT-PCR were visualized on 1.5 % agarose gel electrophoresis. From this study we obtained a 1323 bp fragment cDNA.</p><p> </p><p><strong>Keywords: </strong><em>Capsicum frutescens</em><em> </em>L. cv<em>.</em>Cakra Hijau; <em>Pun1 </em>gene; synthesis of cDNA.</p>
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Martı́n-Castellanos, Cristina, Miguel A. Blanco, José M. de Prada, and Sergio Moreno. "The puc1 Cyclin Regulates the G1 Phase of the Fission Yeast Cell Cycle in Response to Cell Size." Molecular Biology of the Cell 11, no. 2 (February 2000): 543–54. http://dx.doi.org/10.1091/mbc.11.2.543.
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Eukaryotic cells coordinate cell size with cell division by regulating the length of the G1 and G2 phases of the cell cycle. In fission yeast, the length of the G1 phase depends on a precise balance between levels of positive (cig1, cig2, puc1, and cdc13 cyclins) and negative (rum1 and ste9-APC) regulators of cdc2. Early in G1, cyclin proteolysis and rum1 inhibition keep the cdc2/cyclin complexes inactive. At the end of G1, the balance is reversed and cdc2/cyclin activity down-regulates both rum1 and the cyclin-degrading activity of the APC. Here we present data showing that the puc1 cyclin, a close relative of the Cln cyclins in budding yeast, plays an important role in regulating the length of G1. Fission yeast cells lacking cig1 and cig2 have a cell cycle distribution similar to that of wild-type cells, with a short G1 and a long G2. However, when thepuc1 + gene is deleted in this genetic background, the length of G1 is extended and these cells undergo S phase with a greater cell size than wild-type cells. This G1 delay is completely abolished in cells lacking rum1. Cdc2/puc1 function may be important to down-regulate the rum1 Cdk inhibitor at the end of G1.
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Li, Heng, Hui Shi, Hong Wang, Zhiqiang Zhu, Xu Li, Yongxiang Gao, Yingji Cui, Liwen Niu, and Maikun Teng. "Crystal structure of the two N-terminal RRM domains of Pub1 and the poly(U)-binding properties of Pub1." Journal of Structural Biology 171, no. 3 (September 2010): 291–97. http://dx.doi.org/10.1016/j.jsb.2010.04.014.
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Shin, Na-Hyun, Jae-Hyuk Han, Su Jang, Kihwan Song, Hee-Jong Koh, Jong-Hee Lee, Soocheul Yoo, and Joong Hyoun Chin. "Early Vigor of a Pyramiding Line Containing Two Quantitative Trait Loci, Phosphorus Uptake 1 (Pup1) and Anaerobic Germination 1 (AG1) in Rice (O. Sativa L.)." Agriculture 10, no. 10 (October 1, 2020): 453. http://dx.doi.org/10.3390/agriculture10100453.
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Direct-seeded rice is one of the solutions against the issues of limited labor and time in the rice cropping system. Improved useful traits, such as fertilizer uptake and anaerobic germination, are needed to increase yield and efficiency in the direct seeding system in rice. Pup1 (Phosphorous uptake1) containing PSTOL1 is useful in improving the phosphate uptake under rainfed/upland conditions. OsTPP7 is the major gene of AG1 (Anaerobic Germination), which shows anaerobic germination. IR64-Pup1-AG1 (I-PA) was developed by pyramiding Pup1 and AG1. Around 20% of the chromosomal segments from the donor remained in I-PA. Phenotypic analysis revealed that I-PA showed better phenotypic performance under low and normal P conditions by enhancing the root system and tiller numbers during the early stage. Significantly better P uptake capacity of I-PA was observed upon a P-supplied soil condition. The coleoptile length and germination rate of I-PA showed tolerance under anaerobic-germinated conditions. PSTOL1 and OsTPP7 were independently expressed under different P conditions of soils, as well as anaerobic conditions. The newly developed breeding lines, I-PA, showed early vigor capacity through a high number of tillers, better P uptake, and germination in low-oxygen conditions. It will be a useful and improved breeding line for direct seeding rice breeding programs.