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Journal articles on the topic 'PABP'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 May 2024

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1

Dufresne, Philippe J., Eliane Ubalijoro, Marc G. Fortin, and Jean-François Laliberté. "Arabidopsis thaliana class II poly(A)-binding proteins are required for efficient multiplication of turnip mosaic virus." Journal of General Virology 89, no. 9 (2008): 2339–48. http://dx.doi.org/10.1099/vir.0.2008/002139-0.

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The poly(A)-binding protein (PABP) is an important translation initiation factor that binds to the polyadenylated 3′ end of mRNA. We have previously shown that PABP2 interacts with the RNA-dependent RNA polymerase (RdRp) and VPg-Pro of turnip mosaic virus (TuMV) within virus-induced vesicles. At least eight PABP isoforms are produced in Arabidopsis thaliana, three of which (PABP2, PABP4 and PABP8) are highly and broadly expressed and probably constitute the bulk of PABP required for cellular functions. Upon TuMV infection, an increase in protein and mRNA expression from PAB2, PAB4 and PAB8 gen

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2

Assis, Ludmila A., Moezio V. C. Santos Filho, Joao R. da Cruz Silva, et al. "Identification of novel proteins and mRNAs differentially bound to the Leishmania Poly(A) Binding Proteins reveals a direct association between PABP1, the RNA-binding protein RBP23 and mRNAs encoding ribosomal proteins." PLOS Neglected Tropical Diseases 15, no. 10 (2021): e0009899. http://dx.doi.org/10.1371/journal.pntd.0009899.

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Poly(A) Binding Proteins (PABPs) are major eukaryotic RNA-binding proteins (RBPs) with multiple roles associated with mRNA stability and translation and characterized mainly from multicellular organisms and yeasts. A variable number of PABP homologues are seen in different organisms however the biological reasons for multiple PABPs are generally not well understood. In the unicellular Leishmania, dependent on post-transcriptional mechanisms for the control of its gene expression, three distinct PABPs are found, with yet undefined functional distinctions. Here, using RNA-immunoprecipitation seq

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3

Belostotsky, Dmitry A. "Unexpected Complexity of Poly(A)-Binding Protein Gene Families in Flowering Plants: Three Conserved Lineages That Are at Least 200 Million Years Old and Possible Auto- and Cross-Regulation." Genetics 163, no. 1 (2003): 311–19. http://dx.doi.org/10.1093/genetics/163.1.311.

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Abstract Eukaryotic poly(A)-binding protein (PABP) is a ubiquitous, essential factor involved in mRNA biogenesis, translation, and turnover. Most eukaryotes examined have only one or a few PABPs. In contrast, eight expressed PABP genes are present in Arabidopsis thaliana. These genes fall into three distinct classes, based on highly concordant results of (i) phylogenetic analysis of the amino acid sequences of the encoded proteins, (ii) analysis of the intron number and placement, and (iii) surveys of gene expression patterns. Representatives of each of the three classes also exist in the rice

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4

Drawbridge, J., J. L. Grainger, and M. M. Winkler. "Identification and characterization of the poly(A)-binding proteins from the sea urchin: a quantitative analysis." Molecular and Cellular Biology 10, no. 8 (1990): 3994–4006. http://dx.doi.org/10.1128/mcb.10.8.3994-4006.1990.

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Poly(A)-binding proteins (PABPs) are the best characterized messenger RNA-binding proteins of eucaryotic cells and have been identified in diverse organisms such as mammals and yeasts. The in vitro poly(A)-binding properties of these proteins have been studied intensively; however, little is known about their function in cells. In this report, we show that sea urchin eggs have two molecular weight forms of PABP (molecular weights of 66,000 and 80,000). Each of these has at least five posttranslationally modified forms. Both sea urchin PABPs are found in approximately 1:1 ratios in both cytopla

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5

Drawbridge, J., J. L. Grainger, and M. M. Winkler. "Identification and characterization of the poly(A)-binding proteins from the sea urchin: a quantitative analysis." Molecular and Cellular Biology 10, no. 8 (1990): 3994–4006. http://dx.doi.org/10.1128/mcb.10.8.3994.

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Poly(A)-binding proteins (PABPs) are the best characterized messenger RNA-binding proteins of eucaryotic cells and have been identified in diverse organisms such as mammals and yeasts. The in vitro poly(A)-binding properties of these proteins have been studied intensively; however, little is known about their function in cells. In this report, we show that sea urchin eggs have two molecular weight forms of PABP (molecular weights of 66,000 and 80,000). Each of these has at least five posttranslationally modified forms. Both sea urchin PABPs are found in approximately 1:1 ratios in both cytopla

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6

Gu, Sohyun, Hyung-Min Jeon, Seung Woo Nam, et al. "The flip-flop configuration of the PABP-dimer leads to switching of the translation function." Nucleic Acids Research 50, no. 1 (2021): 306–21. http://dx.doi.org/10.1093/nar/gkab1205.

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Abstract Poly(A)-binding protein (PABP) is a translation initiation factor that interacts with the poly(A) tail of mRNAs. PABP bound to poly(A) stimulates translation by interacting with the eukaryotic initiation factor 4G (eIF4G), which brings the 3′ end of an mRNA close to its 5′ m7G cap structure through consecutive interactions of the 3′-poly(A)–PABP-eIF4G-eIF4E-5′ m7G cap. PABP is a highly abundant translation factor present in considerably larger quantities than mRNA and eIF4G in cells. However, it has not been elucidated how eIF4G, present in limited cellular concentrations, is not sequ

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7

Turtola, Matti, M. Cemre Manav, Ananthanarayanan Kumar, et al. "Three-layered control of mRNA poly(A) tail synthesis in Saccharomyces cerevisiae." Genes & Development 35, no. 17-18 (2021): 1290–303. http://dx.doi.org/10.1101/gad.348634.121.

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Biogenesis of most eukaryotic mRNAs involves the addition of an untemplated polyadenosine (pA) tail by the cleavage and polyadenylation machinery. The pA tail, and its exact length, impacts mRNA stability, nuclear export, and translation. To define how polyadenylation is controlled in S. cerevisiae, we have used an in vivo assay capable of assessing nuclear pA tail synthesis, analyzed tail length distributions by direct RNA sequencing, and reconstituted polyadenylation reactions with purified components. This revealed three control mechanisms for pA tail length. First, we found that the pA bin

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8

Smith, Richard W. P., Tajekesa K. P. Blee, and Nicola K. Gray. "Poly(A)-binding proteins are required for diverse biological processes in metazoans." Biochemical Society Transactions 42, no. 4 (2014): 1229–37. http://dx.doi.org/10.1042/bst20140111.

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PABPs [poly(A)-binding proteins] bind to the poly(A) tail of eukaryotic mRNAs and are conserved in species ranging from yeast to human. The prototypical cytoplasmic member, PABP1, is a multifunctional RNA-binding protein with roles in global and mRNA-specific translation and stability, consistent with a function as a central regulator of mRNA fate in the cytoplasm. More limited insight into the molecular functions of other family members is available. However, the consequences of disrupting PABP function in whole organisms is less clear, particularly in vertebrates, and even more so in mammals

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9

Álvarez, Enrique, Alfredo Castelló, Luis Menéndez-Arias, and Luis Carrasco. "HIV protease cleaves poly(A)-binding protein." Biochemical Journal 396, no. 2 (2006): 219–26. http://dx.doi.org/10.1042/bj20060108.

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The PABP [poly(A)-binding protein] is able to interact with the 3′ poly(A) tail of eukaryotic mRNA, promoting its translation. Cleavage of PABP by viral proteases encoded by several picornaviruses and caliciviruses plays a role in the abrogation of cellular protein synthesis. We report that infection of MT-2 cells with HIV-1 leads to efficient proteolysis of PABP. Analysis of PABP integrity was carried out in BHK-21 (baby-hamster kidney) and COS-7 cells upon individual expression of the protease from several members of the Retroviridae family, e.g. MoMLV (Moloney murine leukaemia virus), MMTV

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10

Fischer, Karlee, Mikayla Roberts, Scott Roscoe, Yasin Avci, and Sirinart Ananvoranich. "Toxoplasma gondii infection induces the formation of host’s nuclear granules containing poly(A)-binding proteins." Canadian Journal of Microbiology 64, no. 8 (2018): 551–58. http://dx.doi.org/10.1139/cjm-2017-0755.

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To study the mechanism by which human host cells respond to an infection of Toxoplasma gondii, we monitored the level of poly(A)-binding protein (PABP), an indicator of translation. Here, we report an observation of the relocalization of PABPs in human host cells upon T. gondii infection. Notably, the aggregates of PABPs formed upon infection are mainly found in the nucleus, which is a different response from that found after exposure to heat shock. Pyrimethamine treatment of the infected monolayers inhibits the multiplicity of the parasite and reverses the relocalization of PABP aggregates. T

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11

Ozturk, Saffet, and Fatma Uysal. "Poly(A)-binding proteins are required for translational regulation in vertebrate oocytes and early embryos." Reproduction, Fertility and Development 29, no. 10 (2017): 1890. http://dx.doi.org/10.1071/rd16283.

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Poly(A)-binding proteins (PABPs) function in the timely regulation of gene expression during oocyte maturation, fertilisation and early embryo development in vertebrates. To this end, PABPs bind to poly(A) tails or specific sequences of maternally stored mRNAs to protect them from degradation and to promote their translational activities. To date, two structurally different PABP groups have been identified: (1) cytoplasmic PABPs, including poly(A)-binding protein, cytoplasmic 1 (PABPC1), embryonic poly(A)-binding protein (EPAB), induced PABP and poly(A)-binding protein, cytoplasmic 3; and (2)

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12

Stambuk, R. A., and R. T. Moon. "Purification and characterization of recombinant Xenopus poly(A)+-binding protein expressed in a baculovirus system." Biochemical Journal 287, no. 3 (1992): 761–66. http://dx.doi.org/10.1042/bj2870761.

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The poly(A)(+)-binding protein (PABP) is a highly conserved protein that binds to the poly(A)+ tail of mRNAs. PABP has been shown to regulate message stability and translational efficiency, yet the mechanisms remain unknown. To facilitate further dissection of the functions of this protein, we have expressed and purified Xenopus PABP using a baculovirus expression system. At 48 h after infection of insect Spodoptera frugiperda (Sf9) cells with recombinant virus, approx. 3% of cell protein was PABP. Purification of PABP was achieved by affinity chromatography on poly(A)(+)-Sepharose. The purifi

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13

Aguilar, Lisbeth-Carolina, Biplab Paul, Taylor Reiter, et al. "Altered rRNA processing disrupts nuclear RNA homeostasis via competition for the poly(A)-binding protein Nab2." Nucleic Acids Research 48, no. 20 (2020): 11675–94. http://dx.doi.org/10.1093/nar/gkaa964.

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Abstract RNA-binding proteins (RBPs) are key mediators of RNA metabolism. Whereas some RBPs exhibit narrow transcript specificity, others function broadly across both coding and non-coding RNAs. Here, in Saccharomyces cerevisiae, we demonstrate that changes in RBP availability caused by disruptions to distinct cellular processes promote a common global breakdown in RNA metabolism and nuclear RNA homeostasis. Our data shows that stabilization of aberrant ribosomal RNA (rRNA) precursors in an enp1-1 mutant causes phenotypes similar to RNA exosome mutants due to nucleolar sequestration of the pol

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14

Lee, Seung Hwan, Jungsic Oh, Jonghyun Park, et al. "Poly(A) RNA and Paip2 act as allosteric regulators of poly(A)-binding protein." Nucleic Acids Research 42, no. 4 (2013): 2697–707. http://dx.doi.org/10.1093/nar/gkt1170.

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Abstract When bound to the 3′ poly(A) tail of mRNA, poly(A)-binding protein (PABP) modulates mRNA translation and stability through its association with various proteins. By visualizing individual PABP molecules in real time, we found that PABP, containing four RNA recognition motifs (RRMs), adopts a conformation on poly(A) binding in which RRM1 is in proximity to RRM4. This conformational change is due to the bending of the region between RRM2 and RRM3. PABP-interacting protein 2 actively disrupts the bent structure of PABP to the extended structure, resulting in the inhibition of PABP-poly(A

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15

Khaleghpour, Kianoush, Avak Kahvejian, Gregory De Crescenzo, et al. "Dual Interactions of the Translational Repressor Paip2 with Poly(A) Binding Protein." Molecular and Cellular Biology 21, no. 15 (2001): 5200–5213. http://dx.doi.org/10.1128/mcb.21.15.5200-5213.2001.

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ABSTRACT The cap structure and the poly(A) tail of eukaryotic mRNAs act synergistically to enhance translation. This effect is mediated by a direct interaction of eukaryotic initiation factor 4G and poly(A) binding protein (PABP), which brings about circularization of the mRNA. Of the two recently identified PABP-interacting proteins, one, Paip1, stimulates translation, and the other, Paip2, which competes with Paip1 for binding to PABP, represses translation. Here we studied the Paip2-PABP interaction. Biacore data and far-Western analysis revealed that Paip2 contains two binding sites for PA

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16

Safaee, Nozhat, and Kalle Gehring. "Paip1 and Paip2: conformational modulators of PABP." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C422. http://dx.doi.org/10.1107/s2053273314095771.

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Translation is regulated in cells. Key among the different stages of translation, translation initiation is controlled by regulatory interactions of eIFs and also translation regulatory proteins interacting with eIFs and PABP. PABP-interacting protein (Paip) 1 and 2 have been identified as regulatory proteins affecting the rate of translation initiation through their interactions with PABP. These interactions are mediated by the PABP interacting Motifs (PAM) 1 and 2 of Paips. Paip1 enhances the rate of translation while Paip2 suppresses it. To further understand their mechanisms of actions, he

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17

Bernstein, P., S. W. Peltz, and J. Ross. "The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro." Molecular and Cellular Biology 9, no. 2 (1989): 659–70. http://dx.doi.org/10.1128/mcb.9.2.659-670.1989.

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Using an in vitro mRNA decay system, we investigated how poly(A) and its associated poly(A)-binding protein (PABP) affect mRNA stability. Cell extracts used in the decay reactions were depleted of functional PABP either by adding excess poly(A) competitor or by passing the extracts over a poly(A)-Sepharose column. Polyadenylated mRNAs for beta-globin, chloramphenicol acetyltransferase, and simian virus 40 virion proteins were degraded 3 to 10 times faster in reactions lacking PABP than in those containing excess PABP. The addition of purified Saccharomyces cerevisiae or human cytoplasmic PABP

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18

Bernstein, P., S. W. Peltz, and J. Ross. "The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro." Molecular and Cellular Biology 9, no. 2 (1989): 659–70. http://dx.doi.org/10.1128/mcb.9.2.659.

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Using an in vitro mRNA decay system, we investigated how poly(A) and its associated poly(A)-binding protein (PABP) affect mRNA stability. Cell extracts used in the decay reactions were depleted of functional PABP either by adding excess poly(A) competitor or by passing the extracts over a poly(A)-Sepharose column. Polyadenylated mRNAs for beta-globin, chloramphenicol acetyltransferase, and simian virus 40 virion proteins were degraded 3 to 10 times faster in reactions lacking PABP than in those containing excess PABP. The addition of purified Saccharomyces cerevisiae or human cytoplasmic PABP

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19

Kuyumcu-Martinez, N. Muge, Michelle Joachims, and Richard E. Lloyd. "Efficient Cleavage of Ribosome-Associated Poly(A)-Binding Protein by Enterovirus 3C Protease." Journal of Virology 76, no. 5 (2002): 2062–74. http://dx.doi.org/10.1128/jvi.76.5.2062-2074.2002.

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ABSTRACT Poliovirus (PV) causes a rapid and drastic inhibition of host cell cap-dependent protein synthesis during infection while preferentially allowing cap-independent translation of its own genomic RNA via an internal ribosome entry site element. Inhibition of cap-dependent translation is partly mediated by cleavage of an essential translation initiation factor, eIF4GI, during PV infection. In addition to cleavage of eIF4GI, cleavage of eIF4GII and poly(A)-binding protein (PABP) has been recently proposed to contribute to complete host translation shutoff; however, the relative importance

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20

Kikuchi, Keita, Satoru Shimizu, Yoshiteru Sato, Ella Czarina Morishita, and Akio Takénaka. "Crystallization of oligonucleotides containing A-rich repeats suggests a structural contribution to the autoregulation mechanism of PABP translation." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 2 (2012): 185–89. http://dx.doi.org/10.1107/s1744309111052110.

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Eukaryotic poly(A)-binding protein (PABP) commonly binds to the 3′-UTR poly(A) tail of every mRNA, but it also binds to the 5′-UTR of PABP mRNA for autoregulation of its expression. In the sequence of the latter binding site, the contiguous A residues are segmented discretely by the insertion of short pyrimidine oligonucleotides as linkers, so that (A)6–8segments are repeated six times. This differs from the poly(A)-tail sequence, which has a higher binding affinity for PABP. In order to examine whether the A-rich repeats have a functional structure, several RNA/DNA analogues were subjected to

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Yang, H., C. S. Duckett, and T. Lindsten. "iPABP, an inducible poly(A)-binding protein detected in activated human T cells." Molecular and Cellular Biology 15, no. 12 (1995): 6770–76. http://dx.doi.org/10.1128/mcb.15.12.6770.

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The poly(A)-binding protein (PABP) binds to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. PABP is thought to play a role in both translation and mRNA stability. Here we describe the molecular cloning and characterization of an inducible PABP, iPABP, from a cDNA library prepared from activated T cells. iPABP shows 79% sequence identity to PABP at the amino acid level. The RNA binding domains of iPABP and PABP are nearly identical, while their C termini are more divergent. Like PABP, iPABP is primarily localized to the cytoplasm. iPABP is expressed at low levels in resting no

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22

Leelawai, Sumonthip, Pornchai Sathirapanya, and Chitkasaem Suwanrath. "Bell’s Palsy in Pregnancy: A Case Series." Case Reports in Neurology 12, no. 3 (2020): 452–59. http://dx.doi.org/10.1159/000509682.

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The association between pregnancy-associated Bell’s palsy (PABP) and gestational hypertension (GHT), preeclampsia (PE), and eclampsia (EC) remains inconclusive. We aimed to study the characteristics of PABP cases and the neonatal outcomes at our institution. All cases diagnosed with PABP from 2006 to 2016 were identified. Demographic and clinical characteristics including maternal age, previous medical and obstetric illnesses, gestational age at the onset of PABP, the development of PE/EC, GHT, gestational diabetes mellitus (GDM), treatment and outcomes, as well as neonatal health indices and

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23

Kerekatte, Vaishali, Brett D. Keiper, Cornel Badorff, Aili Cai, Kirk U. Knowlton, and Robert E. Rhoads. "Cleavage of Poly(A)-Binding Protein by Coxsackievirus 2A Protease In Vitro and In Vivo: Another Mechanism for Host Protein Synthesis Shutoff?" Journal of Virology 73, no. 1 (1999): 709–17. http://dx.doi.org/10.1128/jvi.73.1.709-717.1999.

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ABSTRACT Infection of cells by picornaviruses of the rhinovirus, aphthovirus, and enterovirus groups results in the shutoff of host protein synthesis but allows viral protein synthesis to proceed. Although considerable evidence suggests that this shutoff is mediated by the cleavage of eukaryotic translation initiation factor eIF4G by sequence-specific viral proteases (2A protease in the case of coxsackievirus), several experimental observations are at variance with this view. Thus, the cleavage of other cellular proteins could contribute to the shutoff of host protein synthesis and stimulation

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24

Smith, Richard W. P., Ross C. Anderson, Osmany Larralde, et al. "Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding." Proceedings of the National Academy of Sciences 114, no. 24 (2017): 6310–15. http://dx.doi.org/10.1073/pnas.1610417114.

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Regulation of mRNA translation is a major control point for gene expression and is critical for life. Of central importance is the complex between cap-bound eukaryotic initiation factor 4E (eIF4E), eIF4G, and poly(A) tail-binding protein (PABP) that circularizes mRNAs, promoting translation and stability. This complex is often targeted to regulate overall translation rates, and also by mRNA-specific translational repressors. However, the mechanisms of mRNA-specific translational activation by RNA-binding proteins remain poorly understood. Here, we address this deficit, focusing on a herpes sim

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25

Gray, Nicola K., Lenka Hrabálková, Jessica P. Scanlon, and Richard W. P. Smith. "Poly(A)-binding proteins and mRNA localization: who rules the roost?" Biochemical Society Transactions 43, no. 6 (2015): 1277–84. http://dx.doi.org/10.1042/bst20150171.

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RNA-binding proteins are often multifunctional, interact with a variety of protein partners and display complex localizations within cells. Mammalian cytoplasmic poly(A)-binding proteins (PABPs) are multifunctional RNA-binding proteins that regulate multiple aspects of mRNA translation and stability. Although predominantly diffusely cytoplasmic at steady state, they shuttle through the nucleus and can be localized to a variety of cytoplasmic foci, including those associated with mRNA storage and localized translation. Intriguingly, PABP sub-cellular distribution can alter dramatically in respo

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Martineau, Yvan, Mélanie C. Derry, Xiaoshan Wang, et al. "Poly(A)-Binding Protein-Interacting Protein 1 Binds to Eukaryotic Translation Initiation Factor 3 To Stimulate Translation." Molecular and Cellular Biology 28, no. 21 (2008): 6658–67. http://dx.doi.org/10.1128/mcb.00738-08.

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ABSTRACT Poly(A)-binding protein (PABP) stimulates translation initiation by binding simultaneously to the mRNA poly(A) tail and eukaryotic translation initiation factor 4G (eIF4G). PABP activity is regulated by PABP-interacting (Paip) proteins. Paip1 binds PABP and stimulates translation by an unknown mechanism. Here, we describe the interaction between Paip1 and eIF3, which is direct, RNA independent, and mediated via the eIF3g (p44) subunit. Stimulation of translation by Paip1 in vivo was decreased upon deletion of the N-terminal sequence containing the eIF3-binding domain and upon silencin

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27

Polacek, Charlotta, Peter Friebe, and Eva Harris. "Poly(A)-binding protein binds to the non-polyadenylated 3′ untranslated region of dengue virus and modulates translation efficiency." Journal of General Virology 90, no. 3 (2009): 687–92. http://dx.doi.org/10.1099/vir.0.007021-0.

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Poly(A)-binding protein (PABP) is a key player in mRNA circularization and translation initiation of polyadenylated mRNAs. It simultaneously binds the 3′ poly(A) tail of an mRNA and eukaryotic initiation factor 4G (eIF4G), which forms part of the translation initiation complex assembling at the 5′end, thus circularizing the RNA molecule and enhancing translation initiation. Here, we report the binding of PABP to the non-polyadenylated 3′end of dengue virus (DENV) RNA. PABP binds the DENV 3′ untranslated region (3′UTR) internally, upstream of the conserved 3′stem–loop near the two dumb-bell str

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Roy, Guylaine, Gregory De Crescenzo, Kianoush Khaleghpour, Avak Kahvejian, Maureen O'Connor-McCourt, and Nahum Sonenberg. "Paip1 Interacts with Poly(A) Binding Protein through Two Independent Binding Motifs." Molecular and Cellular Biology 22, no. 11 (2002): 3769–82. http://dx.doi.org/10.1128/mcb.22.11.3769-3782.2002.

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ABSTRACT The 3′ poly(A) tail of eukaryotic mRNAs plays an important role in the regulation of translation. The poly(A) binding protein (PABP) interacts with eukaryotic initiation factor 4G (eIF4G), a component of the eIF4F complex, which binds to the 5′ cap structure. The PABP-eIF4G interaction brings about the circularization of the mRNA by joining its 5′ and 3′ termini, thereby stimulating mRNA translation. The activity of PABP is regulated by two interacting proteins, Paip1 and Paip2. To study the mechanism of the Paip1-PABP interaction, far-Western, glutathione S-transferase pull-down, and

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Kuyumcu-Martinez, N. Muge, Marc E. Van Eden, Patrick Younan, and Richard E. Lloyd. "Cleavage of Poly(A)-Binding Protein by Poliovirus 3C Protease Inhibits Host Cell Translation: a Novel Mechanism for Host Translation Shutoff." Molecular and Cellular Biology 24, no. 4 (2004): 1779–90. http://dx.doi.org/10.1128/mcb.24.4.1779-1790.2004.

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ABSTRACT Cleavage of eukaryotic translation initiation factor 4GI (eIF4GI) by viral 2A protease (2Apro) has been proposed to cause severe translation inhibition in poliovirus-infected cells. However, infections containing 1 mM guanidine-HCl result in eIF4GI cleavage but only partial translation shutoff, indicating eIF4GI cleavage is insufficient for drastic translation inhibition. Viral 3C protease (3Cpro) cleaves poly(A)-binding protein (PABP) and removes the C-terminal domain (CTD) that interacts with several translation factors. In HeLa cell translation extracts that exhibit cap-poly(A) syn

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Smith, Richard W. P., and Nicola K. Gray. "Poly(A)-binding protein (PABP): a common viral target." Biochemical Journal 426, no. 1 (2010): 1–12. http://dx.doi.org/10.1042/bj20091571.

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Cytoplasmic PABP [poly(A)-binding protein] is a multifunctional protein with well-studied roles in mRNA translation and stability. In the present review, we examine recent evidence that the activity of PABP is altered during infection with a wide range of viruses, bringing about changes in its stability, complex formation and intracellular localization. Targeting of PABP by both RNA and DNA viruses highlights the role of PABP as a central regulator of gene expression.

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Kuyumcu-Martinez, Muge, Gaël Belliot, Stanislav V. Sosnovtsev, Kyeong-Ok Chang, Kim Y. Green, and Richard E. Lloyd. "Calicivirus 3C-Like Proteinase Inhibits Cellular Translation by Cleavage of Poly(A)-Binding Protein." Journal of Virology 78, no. 15 (2004): 8172–82. http://dx.doi.org/10.1128/jvi.78.15.8172-8182.2004.

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ABSTRACT Caliciviruses are single-stranded RNA viruses that cause a wide range of diseases in both humans and animals, but little is known about the regulation of cellular translation during infection. We used two distinct calicivirus strains, MD145-12 (genus Norovirus) and feline calicivirus (FCV) (genus Vesivirus), to investigate potential strategies used by the caliciviruses to inhibit cellular translation. Recombinant 3C-like proteinases (r3CLpro) from norovirus and FCV were found to cleave poly(A)-binding protein (PABP) in the absence of other viral proteins. The norovirus r3CLpro PABP cl

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Wang, Zuoren, and Megerditch Kiledjian. "The Poly(A)-Binding Protein and an mRNA Stability Protein Jointly Regulate an Endoribonuclease Activity." Molecular and Cellular Biology 20, no. 17 (2000): 6334–41. http://dx.doi.org/10.1128/mcb.20.17.6334-6341.2000.

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ABSTRACT We previously identified a sequence-specific erythroid cell-enriched endoribonuclease (ErEN) activity involved in the turnover of the stable α-globin mRNA. We now demonstrate that ErEN activity is regulated by the poly(A) tail. The unadenylated α-globin 3′ untranslated region (3′UTR) was an efficient substrate for ErEN cleavage, while the polyadenylated 3′UTR was inefficiently cleaved in an in vitro decay assay. The influence of the poly(A) tail was mediated through the poly(A)-binding protein (PABP) bound to the poly(A) tail, which can inhibit ErEN activity. ErEN cleavage of an adeny

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Sagliocco, Francis, Benoît Laloo, Bertrand Cosson, et al. "The ARE-associated factor AUF1 binds poly(A) in vitro in competition with PABP." Biochemical Journal 400, no. 2 (2006): 337–47. http://dx.doi.org/10.1042/bj20060328.

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The ARE (AU-rich element) is a post-transcriptional element controlling both mRNA turnover and translation initiation by primarily inducing poly(A) tail shortening. The mechanisms by which the ARE-associated proteins induce deadenylation are still obscure. One possibility among others would be that an ARE–ARE-BP (ARE-binding protein) complex intervenes in the PABP [poly(A)-binding protein]–poly(A) tail association and facilitates poly(A) tail accessibility to deadenylases. Here, we show by several experimental approaches that AUF1 (AU-rich element RNA-binding protein 1)/hnRNP (heterogeneous nu

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Joachims, Michelle, Pieter C. Van Breugel, and Richard E. Lloyd. "Cleavage of Poly(A)-Binding Protein by Enterovirus Proteases Concurrent with Inhibition of Translation In Vitro." Journal of Virology 73, no. 1 (1999): 718–27. http://dx.doi.org/10.1128/jvi.73.1.718-727.1999.

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ABSTRACT Many enteroviruses, members of the familyPicornaviridae, cause a rapid and drastic inhibition of host cell protein synthesis during infection, a process referred to as host cell shutoff. Poliovirus, one of the best-studied enteroviruses, causes marked inhibition of host cell translation while preferentially allowing translation of its own genomic mRNA. An abundance of experimental evidence has accumulated to indicate that cleavage of an essential translation initiation factor, eIF4G, during infection is responsible at least in part for this shutoff. However, evidence from inhibitors o

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Blakqori, Gjon, Ingeborg van Knippenberg, and Richard M. Elliott. "Bunyamwera Orthobunyavirus S-Segment Untranslated Regions Mediate Poly(A) Tail-Independent Translation." Journal of Virology 83, no. 8 (2009): 3637–46. http://dx.doi.org/10.1128/jvi.02201-08.

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ABSTRACT The mRNAs of Bunyamwera virus (BUNV), the prototype of the Bunyaviridae family, possess a 5′ cap structure but lack a 3′ poly(A) tail, a common feature of eukaryotic mRNAs that greatly enhances translation efficiency. Viral mRNAs also contain untranslated regions (UTRs) that flank the coding sequence. Using model virus-like mRNAs that harbor the Renilla luciferase reporter gene, we found that the 3′ UTR of the BUNV small-segment mRNA mediated efficient translation in the absence of a poly(A) tail. Viral UTRs did not increase RNA stability, and polyadenylation did not significantly enh

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Ilkow, Carolina S., Valeria Mancinelli, Martin D. Beatch, and Tom C. Hobman. "Rubella Virus Capsid Protein Interacts with Poly(A)-Binding Protein and Inhibits Translation." Journal of Virology 82, no. 9 (2008): 4284–94. http://dx.doi.org/10.1128/jvi.02732-07.

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ABSTRACT During virus assembly, the capsid proteins of RNA viruses bind to genomic RNA to form nucleocapsids. However, it is now evident that capsid proteins have additional functions that are unrelated to nucleocapsid formation. Specifically, their interactions with cellular proteins may influence signaling pathways or other events that affect virus replication. Here we report that the rubella virus (RV) capsid protein binds to poly(A)-binding protein (PABP), a host cell protein that enhances translational efficiency by circularizing mRNAs. Infection of cells with RV resulted in marked increa

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Gusmita, Yesi, and Rahmi Wiza. "Problematika Guru Pendidikan Agama Islam dan Budi Pekerti Pada Masa Pandemi Covid-19." An-Nuha 1, no. 3 (2021): 337–46. http://dx.doi.org/10.24036/annuha.v1i3.91.

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LPenelitian ini dilatarbelakangi oleh problematika pada pembelajaran Pendidikan Agama Islam dan Budi Pekerti (PABP) yang terjadi pada kelas 8. Penelitian ini bertujuan untuk mendeskripsikan permaslahan pembelajaran PABP yang dilaksanakan oleh guru dan siswa kelas 8 serta solusi bagi permasalahan yang dihadapi. Penelitian ini menggunakan pendekatan kualitatif dengan menggunakan metode studi kasus (case studies). Pengambilan sampel dilakukan dengan teknik purposive sampling . Pengumpulan data dilakukan dengan teknik wawancara, observasi dan dokumentasi. Data dianalisis dengan menggunakan teknik

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Berger, Lloyd C., Jnanankur Bag, and Bruce H. Sells. "Translation of poly(A)-binding protein mRNA is regulated by growth conditions." Biochemistry and Cell Biology 70, no. 9 (1992): 770–78. http://dx.doi.org/10.1139/o92-117.

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Translational efficiency of a minor group of mRNAs is regulated by serum levels in 3T6 fibroblasts. Included within this group is the poly(A)-binding protein (PABP) mRNA. We analyzed the distribution of PABP mRNA in polysome profiles and found a large percentage of this mRNA to be translationally repressed in both actively growing (~ 60%) and resting cells (~ 70%). Elevated serum levels induced a distinct bimodal distribution of this mRNA between actively translated and repressed fractions. Similarly, treatment of cells with low doses of cycloheximide also generated a partial shift of represse

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Ardelean, Radu, Adriana Popa, Ecaterina Stela Drăgan, Corneliu-Mircea Davidescu, and Maria Ignat. "New Polymeric Adsorbents Functionalized with Aminobenzoic Groups for the Removal of Residual Antibiotics." Molecules 27, no. 9 (2022): 2894. http://dx.doi.org/10.3390/molecules27092894.

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In this paper, we present the synthesis of new polymeric adsorbents derived from macroporous chloromethylated styrene–divinylbenzene (DVB) copolymers with different cross-linking degrees functionalized with the following aminobenzoic groups: styrene—6.7% DVB (PAB1), styrene—10% DVB (PAB2), and styrene—15% DVB (PAB3). The new polymeric products, PAB1, PAB2, and PAB3, were characterized by FTIR spectroscopy, thermogravimetric analysis, and EDX, SEM, and BET analysis, respectively. The evolution of the functionalization reaction was followed by FTIR spectroscopy, which revealed a decrease in the

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Bonderoff, Jennifer M., Jennifer L. LaRey, and Richard E. Lloyd. "Cleavage of Poly(A)-Binding Protein by Poliovirus 3C Proteinase Inhibits Viral Internal Ribosome Entry Site-Mediated Translation." Journal of Virology 82, no. 19 (2008): 9389–99. http://dx.doi.org/10.1128/jvi.00006-08.

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ABSTRACT The two enteroviral proteinases, 2A proteinase (2Apro) and 3C proteinase (3Cpro), induce host cell translation shutoff in enterovirus-infected cells by cleaving canonical translation initiation factors. Cleavage of poly(A)-binding protein (PABP) by 3Cpro has been shown to be a necessary component for host translation shutoff. Here we show that 3Cpro inhibits cap-independent translation mediated by the poliovirus internal ribosome entry site (IRES) in a dose-dependent manner in HeLa translation extracts displaying cap-poly(A) synergy. This effect is independent of the stimulatory effec

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da Costa Lima, Tamara D., Danielle M. N. Moura, Christian R. S. Reis, et al. "Functional Characterization of Three Leishmania Poly(A) Binding Protein Homologues with Distinct Binding Properties to RNA and Protein Partners." Eukaryotic Cell 9, no. 10 (2010): 1484–94. http://dx.doi.org/10.1128/ec.00148-10.

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ABSTRACT Trypanosomatid protozoans are reliant on posttranscriptional processes to control gene expression. Regulation occurs at the levels of mRNA processing, stability, and translation, events that may require the participation of the poly(A) binding protein (PABP). Here, we have undertaken a functional study of the three distinct Leishmania major PABP (LmPABP) homologues: the previously described LmPABP1; LmPABP2, orthologous to the PABP described from Trypanosoma species; and LmPABP3, unique to Leishmania. Sequence identity between the three PABPs is no greater than 40%. In assays measurin

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Skabkina, Olga V., Dmitry N. Lyabin, Maxim A. Skabkin, and Lev P. Ovchinnikov. "YB-1 Autoregulates Translation of Its Own mRNA at or prior to the Step of 40S Ribosomal Subunit Joining." Molecular and Cellular Biology 25, no. 8 (2005): 3317–23. http://dx.doi.org/10.1128/mcb.25.8.3317-3323.2005.

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ABSTRACT YB-1 is a member of the numerous families of proteins with an evolutionary ancient cold-shock domain. It is involved in many DNA- and RNA-dependent events and regulates gene expression at different levels. Previously, we found a regulatory element within the 3′ untranslated region (UTR) of YB-1 mRNA that specifically interacted with YB-1 and poly(A)-binding protein (PABP); we also showed that PABP positively affected YB-1 mRNA translation in a poly(A) tail-independent manner (O. V. Skabkina, M. A. Skabkin, N. V. Popova, D. N. Lyabin, L. O. Penalva, and L. P. Ovchinnikov, J. Biol. Chem

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Harb, Maya, Michelle M. Becker, Damien Vitour, et al. "Nuclear Localization of Cytoplasmic Poly(A)-Binding Protein upon Rotavirus Infection Involves the Interaction of NSP3 with eIF4G and RoXaN." Journal of Virology 82, no. 22 (2008): 11283–93. http://dx.doi.org/10.1128/jvi.00872-08.

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ABSTRACT Rotavirus nonstructural protein NSP3 interacts specifically with the 3′ end of viral mRNAs, with the eukaryotic translation initiation factor eIF4G, and with RoXaN, a cellular protein of yet-unknown function. By evicting cytoplasmic poly(A) binding protein (PABP-C1) from translation initiation complexes, NSP3 shuts off the translation of cellular polyadenylated mRNAs. We show here that PABP-C1 evicted from eIF4G by NSP3 accumulates in the nucleus of rotavirus-infected cells. Through modeling of the NSP3-RoXaN complex, we have identified mutations in NSP3 predicted to interrupt its int

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Fabian, Marc R., Géraldine Mathonnet, Thomas Sundermeier, et al. "Mammalian miRNA RISC Recruits CAF1 and PABP to Affect PABP-Dependent Deadenylation." Molecular Cell 35, no. 6 (2009): 868–80. http://dx.doi.org/10.1016/j.molcel.2009.08.004.

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Dobrikova, Elena, Mayya Shveygert, Robert Walters, and Matthias Gromeier. "Herpes Simplex Virus Proteins ICP27 and UL47 Associate with Polyadenylate-Binding Protein and Control Its Subcellular Distribution." Journal of Virology 84, no. 1 (2009): 270–79. http://dx.doi.org/10.1128/jvi.01740-09.

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ABSTRACT Human pathogenic viruses manipulate host cell translation machinery to ensure efficient expression of viral genes and to thwart host cell protein synthesis. Viral strategies include cleaving translation factors, manipulating translation factor abundance and recruitment into translation initiation complexes, or expressing viral translation factor analogs. Analyzing translation factors in herpes simplex virus type 1 (HSV-1)-infected HeLa cells, we found diminished association of the polyadenylate-binding protein (PABP) with the cap-binding complex. Although total PABP levels were unchan

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Wang, Zuoren, Nancy Day, Panayiota Trifillis, and Megerditch Kiledjian. "An mRNA Stability Complex Functions with Poly(A)-Binding Protein To Stabilize mRNA In Vitro." Molecular and Cellular Biology 19, no. 7 (1999): 4552–60. http://dx.doi.org/10.1128/mcb.19.7.4552.

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ABSTRACT The stable globin mRNAs provide an ideal system for studying the mechanism governing mammalian mRNA turnover. α-Globin mRNA stability is dictated by sequences in the 3′ untranslated region (3′UTR) which form a specific ribonucleoprotein complex (α-complex) whose presence correlates with mRNA stability. One of the major protein components within this complex is a family of two polycytidylate-binding proteins, αCP1 and αCP2. Using an in vitro-transcribed and polyadenylated α-globin 3′UTR, we have devised an in vitro mRNA decay assay which reproduces the α-complex-dependent mRNA stabilit

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Melo, Eduardo O., Rafael Dhalia, Cezar Martins de Sa, Nancy Standart, and Osvaldo P. de Melo Neto. "Identification of a C-terminal Poly(A)-binding Protein (PABP)-PABP Interaction Domain." Journal of Biological Chemistry 278, no. 47 (2003): 46357–68. http://dx.doi.org/10.1074/jbc.m307624200.

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Lu, Pong-Jeu, Chi-Fu Jeffrey Yang, Meng-Yu Wu, Chun-Hao Hung, Ming-Yao Chan, and Tzu-Cheng Hsu. "Wave intensity analysis of para-aortic counterpulsation." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 7 (2012): H1481—H1491. http://dx.doi.org/10.1152/ajpheart.00551.2011.

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Wave intensity analysis (WIA) was used to delineate and maximize the efficacy of a newly developed para-aortic blood pump (PABP). The intra-aortic balloon pump (IABP) was employed as the comparison benchmark. Acute porcine experiments using eight pigs, randomly divided into IABP ( n = 4) and PABP ( n = 4) groups, were conducted to compare the characteristics of intra- and para-aortic counterpulsation. We measured pressure and velocity with probes installed in the left anterior descending coronary artery and aorta, during and without PABP assistance. Wave intensity for aortic and left coronary

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Kawahara, Hironori, Takao Imai, Hiroaki Imataka, Masafumi Tsujimoto, Ken Matsumoto, and Hideyuki Okano. "Neural RNA-binding protein Musashi1 inhibits translation initiation by competing with eIF4G for PABP." Journal of Cell Biology 181, no. 4 (2008): 639–53. http://dx.doi.org/10.1083/jcb.200708004.

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Musashi1 (Msi1) is an RNA-binding protein that is highly expressed in neural stem cells. We previously reported that Msi1 contributes to the maintenance of the immature state and self-renewal activity of neural stem cells through translational repression of m-Numb. However, its translation repression mechanism has remained unclear. Here, we identify poly(A) binding protein (PABP) as an Msi1-binding protein, and find Msi1 competes with eIF4G for PABP binding. This competition inhibits translation initiation of Msi1's target mRNA. Indeed, deletion of the PABP-interacting domain in Msi1 abolishes

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Burd, C. G., E. L. Matunis, and G. Dreyfuss. "The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities." Molecular and Cellular Biology 11, no. 7 (1991): 3419–24. http://dx.doi.org/10.1128/mcb.11.7.3419-3424.1991.

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The poly(A)-binding protein (PABP) is the major mRNA-binding protein in eukaryotes, and it is essential for viability of the yeast Saccharomyces cerevisiae. The amino acid sequence of the protein indicates that it consists of four ribonucleoprotein consensus sequence-containing RNA-binding domains (RBDs I, II, III, and IV) and a proline-rich auxiliary domain at the carboxyl terminus. We produced different parts of the S. cerevisiae PABP and studied their binding to poly(A) and other ribohomopolymers in vitro. We found that none of the individual RBDs of the protein bind poly(A) specifically or

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