Relevant bibliographies by topics / 5’UTR binding proteins

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Academic literature on the topic '5’UTR binding proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "5’UTR binding proteins"

1

Stripecke, R., C. C. Oliveira, J. E. McCarthy, and M. W. Hentze. "Proteins binding to 5' untranslated region sites: a general mechanism for translational regulation of mRNAs in human and yeast cells." Molecular and Cellular Biology 14, no. 9 (September 1994): 5898–909. http://dx.doi.org/10.1128/mcb.14.9.5898.

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We demonstrate that a bacteriophage protein and a spliceosomal protein can be converted into eukaryotic translational repressor proteins. mRNAs with binding sites for the bacteriophage MS2 coat protein or the spliceosomal human U1A protein were expressed in human HeLa cells and yeast. The presence of the appropriate binding protein resulted in specific, dose-dependent translational repression when the binding sites were located in the 5' untranslated region (UTR) of the reporter mRNAs. Neither mRNA export from the nucleus to the cytoplasm nor mRNA stability was demonstrably affected by the binding proteins. The data thus reveal a general mechanism for translational regulation: formation of mRNA-protein complexes in the 5' UTR controls translation initiation by steric blockage of a sensitive step in the initiation pathway. Moreover, the findings establish the basis for novel strategies to study RNA-protein interactions in vivo and to clone RNA-binding proteins.
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Stripecke, R., C. C. Oliveira, J. E. McCarthy, and M. W. Hentze. "Proteins binding to 5' untranslated region sites: a general mechanism for translational regulation of mRNAs in human and yeast cells." Molecular and Cellular Biology 14, no. 9 (September 1994): 5898–909. http://dx.doi.org/10.1128/mcb.14.9.5898-5909.1994.

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We demonstrate that a bacteriophage protein and a spliceosomal protein can be converted into eukaryotic translational repressor proteins. mRNAs with binding sites for the bacteriophage MS2 coat protein or the spliceosomal human U1A protein were expressed in human HeLa cells and yeast. The presence of the appropriate binding protein resulted in specific, dose-dependent translational repression when the binding sites were located in the 5' untranslated region (UTR) of the reporter mRNAs. Neither mRNA export from the nucleus to the cytoplasm nor mRNA stability was demonstrably affected by the binding proteins. The data thus reveal a general mechanism for translational regulation: formation of mRNA-protein complexes in the 5' UTR controls translation initiation by steric blockage of a sensitive step in the initiation pathway. Moreover, the findings establish the basis for novel strategies to study RNA-protein interactions in vivo and to clone RNA-binding proteins.
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Kulkarni, Shardul D., Bhavana Muralidharan, Amaresh C. Panda, Baskar Bakthavachalu, Arya Vindu, and Vasudevan Seshadri. "Glucose-stimulated Translation Regulation of Insulin by the 5′ UTR-binding Proteins." Journal of Biological Chemistry 286, no. 16 (February 28, 2011): 14146–56. http://dx.doi.org/10.1074/jbc.m110.190553.

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Mbella, E. G. Mbongolo, S. Bertrand, G. Huez, and J. N. Octave. "A GG Nucleotide Sequence of the 3′ Untranslated Region of Amyloid Precursor Protein mRNA Plays a Key Role in the Regulation of Translation and the Binding of Proteins." Molecular and Cellular Biology 20, no. 13 (July 1, 2000): 4572–79. http://dx.doi.org/10.1128/mcb.20.13.4572-4579.2000.

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ABSTRACT The alternative polyadenylation of the mRNA encoding the amyloid precursor protein (APP) involved in Alzheimer's disease generates two molecules, with the first of these containing 258 additional nucleotides in the 3′ untranslated region (3′UTR). We have previously shown that these 258 nucleotides increase the translation of APP mRNA injected in Xenopus oocytes (5). Here, we demonstrate that this mechanism occurs in CHO cells as well. We also present evidence that the 3′UTR containing 8 nucleotides more than the short 3′UTR allows the recovery of an efficiency of translation similar to that of the long 3′UTR. Moreover, the two guanine residues located at the 3′ ends of these 8 nucleotides play a key role in the translational control. Using gel retardation mobility shift assay, we show that proteins from Xenopus oocytes, CHO cells, and human brain specifically bind to the short 3′UTR but not to the long one. The two guanine residues involved in the translational control inhibit this specific binding by 65%. These results indicate that there is a correlation between the binding of proteins to the 3′UTR of APP mRNA and the efficiency of mRNA translation, and that a GG motif controls both binding of proteins and translation.
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Kash, John C., Dawn M. Cunningham, Maria W. Smit, Youngwoo Park, David Fritz, Jeffrey Wilusz, and Michael G. Katze. "Selective Translation of Eukaryotic mRNAs: Functional Molecular Analysis of GRSF-1, a Positive Regulator of Influenza Virus Protein Synthesis." Journal of Virology 76, no. 20 (October 15, 2002): 10417–26. http://dx.doi.org/10.1128/jvi.76.20.10417-10426.2002.

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ABSTRACT To understand the regulation of cap-dependent translation initiation mediated by specific 5′ untranslated region (UTR) RNA-protein interactions in mammalian cells, we have studied the selective translation of influenza virus mRNAs. Previous work has shown that the host cell mRNA binding protein guanine-rich sequence factor 1 (GRSF-1) bound specifically to conserved viral 5′ UTR sequences and stimulated translation of viral 5′ UTR-driven mRNAs in vitro. In the present study, we have characterized the functional domains of GRSF-1 and mapped the RNA binding activity of GRSF-1 to RRM 2 (amino acids 194 to 275) with amino-terminal deletion glutathione S-transferase (GST)-GRSF-1 proteins. When these mutants were assayed for functional activity in vitro, deletion of an Ala-rich region (Δ[2-94]) appeared to diminish translational stimulation, while deletion of the Ala-rich region in addition to RRM 1 (Δ[2-194]) resulted in a 4-fold increase in translational activation over wild-type GRSF-1 (an overall 20-fold increase in activity). We have also mapped the GRSF-1 RNA binding site on influenza virus NP and NS1 5′ UTRs, which was determined to be the sequence AGGGU. With polysome fractionation and cDNA microarray analysis, we have identified cellular and viral mRNAs containing putative GRSF-1 binding sites that were transcriptionally up-regulated and selectively recruited to polyribosomes following influenza virus infection. Taken together, these studies demonstrate that RRM 2 is critical for GRSF-1 RNA binding and translational activity. Further, our data suggest GRSF-1 functions by selectively recruiting cellular and viral mRNAs containing 5′ UTR GRSF-1 binding sites to polyribosomes, which is mediated through interactions with cellular proteins.
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Yocupicio-Monroy, Rosa Martha E., Fernando Medina, Jorge Reyes-del Valle, and Rosa M. del Angel. "Cellular Proteins from Human Monocytes Bind to Dengue 4 Virus Minus-Strand 3′ Untranslated Region RNA." Journal of Virology 77, no. 5 (March 1, 2003): 3067–76. http://dx.doi.org/10.1128/jvi.77.5.3067-3076.2003.

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ABSTRACT The synthesis of plus and minus RNA strands of several RNA viruses requires as a first step the interaction of some viral regulatory sequences with cellular and viral proteins. The dengue 4 virus genome, a single-stranded, positive-polarity RNA, is flanked by two untranslated regions (UTR) located in the 5′ and 3′ ends. The 3′UTR in the minus-strand RNA [3′UTR (−)] has been thought to function as a promoter for the synthesis of plus-strand RNA. To study the initial interaction between this 3′UTR and cellular and viral proteins, mobility shift assays were performed, and four ribonucleoprotein complexes (I through IV) were formed when uninfected and infected U937 cells (human monocyte cell line) interacted with the 3′UTR (−) of dengue 4 virus. Cross-linking assays with RNAs containing the complete 3′UTR (−) (nucleotides [nt] 101 to 1) or a partial sequence from nt 101 to 45 and nt 44 to 1 resulted in specific binding of some cellular proteins. Supermobility shift and immunoprecipitation assays demonstrated that the La protein forms part of these complexes. To determine the region in the 3′ UTR that interacted with the La protein, two deletion mutants were generated. The mutant (del-96), with a deletion of nt 96 to 101, was unable to interact with the La protein, suggesting that La interacted with the 5′ portion of the 3′UTR (−). Complex I, which was the main ribonucleoprotein complex formed with the 3′UTR (−) and which had the fastest electrophoretic migration, contained proteins such as calreticulin and protein disulfide isomerase, which constitute important components of the endoplasmic reticulum.
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Nielsen, Jacob, Jan Christiansen, Jens Lykke-Andersen, Anders H. Johnsen, Ulla M. Wewer, and Finn C. Nielsen. "A Family of Insulin-Like Growth Factor II mRNA-Binding Proteins Represses Translation in Late Development." Molecular and Cellular Biology 19, no. 2 (February 1, 1999): 1262–70. http://dx.doi.org/10.1128/mcb.19.2.1262.

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ABSTRACT Insulin-like growth factor II (IGF-II) is a major fetal growth factor. The IGF-II gene generates multiple mRNAs with different 5′ untranslated regions (5′ UTRs) that are translated in a differential manner during development. We have identified a human family of three IGF-II mRNA-binding proteins (IMPs) that exhibit multiple attachments to the 5′ UTR from the translationally regulated IGF-II leader 3 mRNA but are unable to bind to the 5′ UTR from the constitutively translated IGF-II leader 4 mRNA. IMPs contain the unique combination of two RNA recognition motifs and four hnRNP K homology domains and are homologous to the Xenopus Vera and chicken zipcode-binding proteins. IMP localizes to subcytoplasmic domains in a growth-dependent and cell-specific manner and causes a dose-dependent translational repression of IGF-II leader 3 –luciferase mRNA. Mouse IMPs are produced in a burst at embryonic day 12.5 followed by a decline towards birth, and, similar to IGF-II, IMPs are especially expressed in developing epithelia, muscle, and placenta in both mouse and human embryos. The results imply that cytoplasmic 5′ UTR-binding proteins control IGF-II biosynthesis during late mammalian development.
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Huang, Peiyong, and Michael M. C. Lai. "Heterogeneous Nuclear Ribonucleoprotein A1 Binds to the 3′-Untranslated Region and Mediates Potential 5′-3′-End Cross Talks of Mouse Hepatitis Virus RNA." Journal of Virology 75, no. 11 (June 1, 2001): 5009–17. http://dx.doi.org/10.1128/jvi.75.11.5009-5017.2001.

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ABSTRACT The 3′-untranslated region (3′-UTR) of mouse hepatitis virus (MHV) RNA regulates the replication of and transcription from the viral RNA. Several host cell proteins have previously been shown to interact with this regulatory region. By immunoprecipitation of UV-cross-linked cellular proteins and in vitro binding of the recombinant protein, we have identified the major RNA-binding protein species as heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1). A strong hnRNP A1-binding site was located 90 to 170 nucleotides from the 3′ end of MHV RNA, and a weak binding site was mapped at nucleotides 260 to 350 from the 3′ end. These binding sites are complementary to the sites on the negative-strand RNA that bind another cellular protein, polypyrimidine tract-binding protein (PTB). Mutations that affect PTB binding to the negative strand of the 3′-UTR also inhibited hnRNP A1 binding on the positive strand, indicating a possible relationship between these two proteins. Defective-interfering RNAs containing a mutated hnRNP A1-binding site have reduced RNA transcription and replication activities. Furthermore, hnRNP A1 and PTB, both of which also bind to the complementary strands at the 5′ end of MHV RNA, together mediate the formation of an RNP complex involving the 5′- and 3′-end fragments of MHV RNA in vitro. These studies suggest that hnRNP A1-PTB interactions provide a molecular mechanism for potential 5′-3′ cross talks in MHV RNA, which may be important for RNA replication and transcription.
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Araujo, Patricia R., Kihoon Yoon, Daijin Ko, Andrew D. Smith, Mei Qiao, Uthra Suresh, Suzanne C. Burns, and Luiz O. F. Penalva. "Before It Gets Started: Regulating Translation at the 5′ UTR." Comparative and Functional Genomics 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/475731.

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Translation regulation plays important roles in both normal physiological conditions and diseases states. This regulation requires cis-regulatory elements located mostly in 5′ and 3′ UTRs and trans-regulatory factors (e.g., RNA binding proteins (RBPs)) which recognize specific RNA features and interact with the translation machinery to modulate its activity. In this paper, we discuss important aspects of 5′ UTR-mediated regulation by providing an overview of the characteristics and the function of the main elements present in this region, like uORF (upstream open reading frame), secondary structures, and RBPs binding motifs and different mechanisms of translation regulation and the impact they have on gene expression and human health when deregulated.
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Leathers, V., R. Tanguay, M. Kobayashi, and D. R. Gallie. "A phylogenetically conserved sequence within viral 3' untranslated RNA pseudoknots regulates translation." Molecular and Cellular Biology 13, no. 9 (September 1993): 5331–47. http://dx.doi.org/10.1128/mcb.13.9.5331.

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Both the 68-base 5' leader (omega) and the 205-base 3' untranslated region (UTR) of tobacco mosaic virus (TMV) promote efficient translation. A 35-base region within omega is necessary and sufficient for the regulation. Within the 3' UTR, a 52-base region, composed of two RNA pseudoknots, is required for regulation. These pseudoknots are phylogenetically conserved among seven viruses from two different viral groups and one satellite virus. The pseudoknots contained significant conservation at the secondary and tertiary levels and at several positions at the primary sequence level. Mutational analysis of the sequences determined that the primary sequence in several conserved positions, particularly within the third pseudoknot, was essential for function. The higher-order structure of the pseudoknots was also required. Both the leader and the pseudoknot region were specifically recognized by, and competed for, the same proteins in extracts made from carrot cell suspension cells and wheat germ. Binding of the proteins is much stronger to omega than the pseudoknot region. Synergism was observed between the TMV 3' UTR and the cap and to a lesser extent between omega and the 3' UTR. The functional synergism and the protein binding data suggest that the cap, TMV 5' leader, and 3' UTR interact to establish an efficient level of translation.
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Dissertations / Theses on the topic "5’UTR binding proteins"

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Renner, Sonja. "Identification of ADAM10 5`UTR binding proteins." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-170738.

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Renner, Sonja [Verfasser], and Christian [Akademischer Betreuer] Haass. "Identification of ADAM10 5`UTR binding proteins : the RNA-binding protein Unr is involved in ADAM10 mRNA stability / Sonja Renner. Betreuer: Christian Haass." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2014. http://d-nb.info/1053618514/34.

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Song, Xiaomin. "Distribution and molecular characterization of 3'-UTR binding proteins specific to the (U)¦1¦5 region of Cas-1 gene." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0013/MQ28664.pdf.

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Abaza, Irina. "Drosophila UNR: a factor involved in the translational regulation of dosage compensation." Doctoral thesis, Universitat Pompeu Fabra, 2006. http://hdl.handle.net/10803/78125.

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Dosage compensation is a mechanism that equalizes the expression of X-linked genes in those organisms in which males and females differ in the number of X chromosomes. In Drosophila melanogaster, dosage compensation is achieved by up-regulating the transcription of the single male X chromosome. This effect is mediated by a chromatin remodeling complex known as the Male Specific Lethal (MSL) complex or Dosage Compensation Complex (DCC). In female flies, dosage compensation is inhibited primarily because of the translational repression of the mRNA encoding one of the DCC subunits, MSL-2, by the female-specific RNA binding protein Sex-lethal (SXL). To inhibit translation, SXL binds to poly(U) stretches present in both the 5’ and 3’ UTRs of msl-2 mRNA. Sequences adjacent to those SXL-binding sites in the 3´UTR are also required for translation inhibition and are bound by co-repression. In this thesis work, we have designed an affinity chromatography assay to isolate the putative co-repressor(s), and have identified the protein Upstream of N-ras (UNR). Drosophila UNR (dUNR) is an ubiquitous, conserved protein that contains 5 cold shock domains (CSD) and a glutamine- (Q) rich amino- terminal extension. We show that dUNR is a necessary co-factor for SXL-mediated msl-2 repression. SXL recruits dUNR to the 3’ UTR of msl-2 mRNA, imparting a sex-specific function to this ubiquitous protein. Domain mapping experiments indicate that dUNR interacts with SXL and msl-2 mRNA through CSD1, and that the domains for translation inhibition and SXL interaction can be distinguished. Our data indicate that the Q-rich domain, together with CSDs 1 and 2, plays an important role in translational repression, and suggest that factors in addition to dUNR and SXL are required for repression of msl-2 mRNA. Using a combination of UNR immunoprecipitation and microarray analysis, we have identified the mRNAs that are bound to dUNR in male and female flies. Our results suggest that dUNR is not only a novel regulator of dosage compensation, but also a general post-transcriptional regulator of gene expression.
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Comandur, Roopa. "Structure of Retroviral 5′-Untranslated Regions and Interactions with Host and Viral Proteins." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu148060178765983.

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Wang, Linya, and 王琳雅. "Poly(C)-binding protein 2 Interacts with sequences Required for Viral Replication in HCV 5’UTR and Directs HCV RNA Replication through Circularizing the Viral Genome." Thesis, 2011. http://ndltd.ncl.edu.tw/handle/03053232058243201104.

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博士
國立臺灣大學
微生物學研究所
99
Sequences in the 5’-untranslated region (5’UTR) of hepatitis C virus (HCV) RNA is important for modulating both translation and RNA replication. Translation of the HCV genome depends on an internal ribosome entry site (IRES) located within the 341-nucleotide 5’-UTR, while RNA replication requires a smaller region. A question arises whether the replication and translation functions require different regions of 5’-UTR and different sets of RNA-binding proteins. Here we showed that the 5’-most 157 nucleotides of HCV RNA is the minimum 5’-UTR for RNA replication, which partially overlaps with IRES. Both stem-loops 1 and 2 of 5’-UTR are essential for RNA replication, whereas stem-loop 1 is not required for translation. We also found that poly(C)-binding protein 2 (PCBP2) bound to the replication region of 5’UTR and associated with detergent-resistant membrane fractions, which is the site of HCV replication complex. Knock-down of PCBP2 by shRNA decreased the amounts of HCV RNA and nonstructural proteins. Antibody-mediated blocking of PCBP2 reduced HCV RNA replication in vitro, indicating that PCBP2 is directly involved in HCV RNA replication. Furthermore, PCBP2 knockdown reduced IRES-dependent translation preferentially from a dual reporter plasmid, suggesting that PCBP2 also regulated IRES activity. These findings indicate that PCBP2 participates in both HCV RNA replication and translation. Moreover, PCBP2 interacts with HCV 5’UTR and 3’UTR RNA fragments to form an RNA-protein complex and induces circularization of HCV RNA as revealed by electron microscopy. This study thus demonstrates the mechanism of participation of PCBP2 in HCV translation and replication and provides the physical evidence for HCV RNA circularization through 5’ and 3’-UTR interaction.
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Conference papers on the topic "5’UTR binding proteins"

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Bell, Brett J., and Sherry L. Voytik-Harbin. "Multiaxial Study of Fibroblast Biomechanics in a 3D Collagen Matrix." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206722.

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It is becoming increasingly evident, that of the signaling modalities relevant to the cell-extracellular matrix (ECM) microenvironment, the mechanical component is a very important mediator of cell behavior (reviewed in [1, 2]). Indeed, proliferation, ECM protein expression (collagen), matrix metalloproteinase (MMP) levels, migration, and stem cell differentiation, have all been shown to be affected by mechanical environmental cues [3, 4]. Although the importance of physical signaling mechanisms has been well established, the bulk of this work has yet to be translated to a more physiologic 3D microenvironment [1]. Self-assembling collagen matrices provide a biochemically, biophysically relevant 3D model of soft tissues in which biomechanical studies can be performed [5, 6]. It is with this 3D tissue model in mind, that a biaxial mechanical testing system (BMTS) was devised, built, tested, and applied to the study of cell-ECM biomechanics. The completion of this device has enabled us, to undertake a multi-scale, multidimensional study of cell-ECM mechanics. Hierarchical quantification of cell and ECM strains using digital image correlation (DIC) facilitate a more complete understanding of the mechanical response of cells to macroscopic loads and deformations. Furthermore, transfection of cells with GFP tagged actin binding protein utrophin (UTR-GFP) enables qualitative assessment of cytoskeletal deformations [7].
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