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Relevant bibliographies by topics / Heterogeneous-Nuclear Ribonucleoprotein U

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Academic literature on the topic 'Heterogeneous-Nuclear Ribonucleoprotein U'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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Journal articles on the topic "Heterogeneous-Nuclear Ribonucleoprotein U"

1

Kawano, Shinji, Mary Miyaji, Shoko Ichiyasu, Kimiko M. Tsutsui, and Ken Tsutsui. "Regulation of DNA Topoisomerase IIβ through RNA-dependent Association with Heterogeneous Nuclear Ribonucleoprotein U (hnRNP U)." Journal of Biological Chemistry 285, no. 34 (June 16, 2010): 26451–60. http://dx.doi.org/10.1074/jbc.m110.112979.

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2

Godbout, Roseline, Margaret Hale, and Dwayne Bisgrove. "A human DEAD box protein with partial homology to heterogeneous nuclear ribonucleoprotein U." Gene 138, no. 1-2 (January 1994): 243–45. http://dx.doi.org/10.1016/0378-1119(94)90816-8.

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3

Eggert, Heike, Martin Schulz, Frank O. Fackelmayer, Rainer Renkawitz, and Martin Eggert. "Effects of the heterogeneous nuclear ribonucleoprotein U (hnRNP U/SAF-A) on glucocorticoid-dependent transcription in vivo." Journal of Steroid Biochemistry and Molecular Biology 78, no. 1 (July 2001): 59–65. http://dx.doi.org/10.1016/s0960-0760(01)00074-7.

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4

Winteringham, Louise N., Raelene Endersby, Simon Kobelke, Ross K. McCulloch, James H. Williams, Justin Stillitano, Scott M. Cornwall, Evan Ingley, and S. Peter Klinken. "Myeloid Leukemia Factor 1 Associates with a Novel Heterogeneous Nuclear Ribonucleoprotein U-like Molecule." Journal of Biological Chemistry 281, no. 50 (September 28, 2006): 38791–800. http://dx.doi.org/10.1074/jbc.m605401200.

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5

von Kries, Jens P., Friedrich Buck, and Wolf H. Sträting. "Chicken MAR binding protein p120 is identical to human heterogeneous nuclear ribonucleoprotein (hnRNP) U." Nucleic Acids Research 22, no. 7 (1994): 1215–20. http://dx.doi.org/10.1093/nar/22.7.1215.

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6

Gupta, Ashim K., Judith A. Drazba, and Amiya K. Banerjee. "Specific Interaction of Heterogeneous Nuclear Ribonucleoprotein Particle U with the Leader RNA Sequence of Vesicular Stomatitis Virus." Journal of Virology 72, no. 11 (November 1, 1998): 8532–40. http://dx.doi.org/10.1128/jvi.72.11.8532-8540.1998.

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ABSTRACT The 3′ ends of the genome and antigenome RNA of vesicular stomatitis virus (VSV) serve as the promoter sites for the RNA-dependent RNA polymerase in the initiation of transcription and replication, respectively. The leader RNA, the first transcript synthesized during the RNA synthetic step, contains sequences to initiate encapsidation with the nucleocapsid protein, which is a prerequisite for replication. It also plays a role in the inhibition of cellular RNA synthesis. To search for a specific cellular factor(s) which may interact with the leader RNA sequences and regulate these processes, we used a gel mobility shift assay to identify such a protein(s). By using nuclear extract, it was found that in addition to the previously reported La protein, a 120-kDa nuclear protein specifically interacts with the leader RNA. Biochemical and immunological studies identified the 120-kDa protein as heterogeneous nuclear ribonucleoprotein particle U (hnRNP U), which is involved in pre-mRNA processing. We also demonstrate that hnRNP U is associated with the leader RNA in the nuclei of VSV-infected cells and also packaged within the purified virions. By double immunofluorescence labeling and confocal microscopy, hnRNP U appears to colocalize with the virus in the cytoplasm of infected cells. These results strongly suggest that hnRNP U plays an important role in the life cycle of VSV.

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7

Swanson, M. S., and G. Dreyfuss. "Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities." Molecular and Cellular Biology 8, no. 5 (May 1988): 2237–41. http://dx.doi.org/10.1128/mcb.8.5.2237.

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Several proteins of heterogeneous nuclear ribonucleoprotein (hnRNP) particles display very high binding affinities for different ribonucleotide homopolymers. The specificity of some of these proteins at high salt concentrations and in the presence of heparin allows for their rapid one-step purification from HeLa nucleoplasm. We show that the hnRNP C proteins are poly(U)-binding proteins and compare their specificity to that of the previously described cytoplasmic poly(A)-binding protein. These findings provide a useful tool for the classification and purification of hnRNP proteins from various tissues and organisms and indicate that different hnRNP proteins have different RNA-binding specificities.

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8

Swanson, M. S., and G. Dreyfuss. "Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities." Molecular and Cellular Biology 8, no. 5 (May 1988): 2237–41. http://dx.doi.org/10.1128/mcb.8.5.2237-2241.1988.

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Several proteins of heterogeneous nuclear ribonucleoprotein (hnRNP) particles display very high binding affinities for different ribonucleotide homopolymers. The specificity of some of these proteins at high salt concentrations and in the presence of heparin allows for their rapid one-step purification from HeLa nucleoplasm. We show that the hnRNP C proteins are poly(U)-binding proteins and compare their specificity to that of the previously described cytoplasmic poly(A)-binding protein. These findings provide a useful tool for the classification and purification of hnRNP proteins from various tissues and organisms and indicate that different hnRNP proteins have different RNA-binding specificities.

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9

Mondal, Samiran, Nasim A. Begum, Wenjun Hu, and Tasuku Honjo. "Functional requirements of AID’s higher order structures and their interaction with RNA-binding proteins." Proceedings of the National Academy of Sciences 113, no. 11 (February 29, 2016): E1545—E1554. http://dx.doi.org/10.1073/pnas.1601678113.

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Activation-induced cytidine deaminase (AID) is essential for the somatic hypermutation (SHM) and class-switch recombination (CSR) of Ig genes. Although both the N and C termini of AID have unique functions in DNA cleavage and recombination, respectively, during SHM and CSR, their molecular mechanisms are poorly understood. Using a bimolecular fluorescence complementation (BiFC) assay combined with glycerol gradient fractionation, we revealed that the AID C terminus is required for a stable dimer formation. Furthermore, AID monomers and dimers form complexes with distinct heterogeneous nuclear ribonucleoproteins (hnRNPs). AID monomers associate with DNA cleavage cofactor hnRNP K whereas AID dimers associate with recombination cofactors hnRNP L, hnRNP U, and Serpine mRNA-binding protein 1. All of these AID/ribonucleoprotein associations are RNA-dependent. We propose that AID’s structure-specific cofactor complex formations differentially contribute to its DNA-cleavage and recombination functions.

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10

Tazi, J., T. Forne, P. Jeanteur, G. Cathala, and C. Brunel. "Mammalian U6 small nuclear RNA undergoes 3' end modifications within the spliceosome." Molecular and Cellular Biology 13, no. 3 (March 1993): 1641–50. http://dx.doi.org/10.1128/mcb.13.3.1641.

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Mammalian U6 small nuclear RNA (snRNA) is heterogeneous with respect to the number of 3' terminal U residues. The major form terminates with five U residues and a 2',3' cyclic phosphate. Because of the presence in HeLa cell nuclear extracts of a terminal uridylyl transferase, a minor form of U6 snRNA is elongated, producing multiple species containing up to 12 U residues. In this study we have used glycerol gradients to demonstrate that these U6 snRNA forms are assembled into U6 ribonucleoprotein (RNP), U4/U6 snRNPs, and U4/U5/U6 tri-snRNP complexes. Furthermore, glycerol gradients combined with affinity selection of biotinylated pre-mRNAs led us to show that elongated forms of U6 snRNAs enter the spliceosome and that some of these become shortened with time to a single species having the same characteristics as the major form of U6 snRNA present in mammalian nuclear extracts. We propose that this elongation-shortening process is related to the function of U6 snRNA in mammalian pre-mRNA splicing.

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Dissertations / Theses on the topic "Heterogeneous-Nuclear Ribonucleoprotein U"

1

Wang, Han [Verfasser]. "Function of Heterogeneous Nuclear Ribonucleoprotein U and related MicroRNAs in Human Coronary Artery Endothelial Cells and Endothelial Microparticles / Han Wang." Bonn : Universitäts- und Landesbibliothek Bonn, 2017. http://d-nb.info/114982168X/34.

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Kolpa, Heather J. "XIST and CoT-1 Repeat RNAs are Integral Components of a Complex Nuclear Scaffold Required to Maintain SAF-A and Modify Chromosome Architecture: A Dissertation." eScholarship@UMMS, 2004. http://escholarship.umassmed.edu/gsbs_diss/825.

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XIST RNA established the precedent for a noncoding RNA that stably associates with and regulates chromatin, however it remains poorly understood how such RNAs structurally associate with the interphase chromosome territory. I demonstrate that transgenic XIST RNA localizes in cis to an autosome as it does to the inactive X chromosome, hence the RNA recognizes a structure common to all chromosomes. I reassess the prevalent thinking in the field that a single protein, Scaffold Attachment Factor-A (SAF-A/hnRNP U), provides a single molecule bridge required to directly tether the RNA to DNA. In an extensive series of experiments in multiple cell types, I examine the effects of SAF-A depletion or different SAF-A mutations on XIST RNA localization, and I force XIST RNA retention at mitosis to examine the effect on SAF-A. I find that SAF-A is not required to localize XIST RNA but is one of multiple proteins involved, some of which frequently become lost or compromised in cancer. I additionally examine SAF-A’s potential role localizing repeat-rich CoT-1 RNA, a class of abundant RNAs that we show tightly and stably localize to euchromatic interphase chromosome territories, but release upon disruption of the nuclear scaffold. Overall, findings suggest that instead of “tethering” chromosomal RNAs to the scaffold, SAF-A is one component of a multi-component matrix/scaffold supporting interphase nuclear architecture. Results indicate that Cot-1 and XIST RNAs form integral components of this scaffold and are required to maintain the chromosomal association of SAF-A, substantially advancing understanding of how chromatin-associated RNAs contribute to nuclear structure.

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3

Kolpa, Heather J. "XIST and CoT-1 Repeat RNAs are Integral Components of a Complex Nuclear Scaffold Required to Maintain SAF-A and Modify Chromosome Architecture: A Dissertation." eScholarship@UMMS, 2016. https://escholarship.umassmed.edu/gsbs_diss/825.

Full text

Abstract:

XIST RNA established the precedent for a noncoding RNA that stably associates with and regulates chromatin, however it remains poorly understood how such RNAs structurally associate with the interphase chromosome territory. I demonstrate that transgenic XIST RNA localizes in cis to an autosome as it does to the inactive X chromosome, hence the RNA recognizes a structure common to all chromosomes. I reassess the prevalent thinking in the field that a single protein, Scaffold Attachment Factor-A (SAF-A/hnRNP U), provides a single molecule bridge required to directly tether the RNA to DNA. In an extensive series of experiments in multiple cell types, I examine the effects of SAF-A depletion or different SAF-A mutations on XIST RNA localization, and I force XIST RNA retention at mitosis to examine the effect on SAF-A. I find that SAF-A is not required to localize XIST RNA but is one of multiple proteins involved, some of which frequently become lost or compromised in cancer. I additionally examine SAF-A’s potential role localizing repeat-rich CoT-1 RNA, a class of abundant RNAs that we show tightly and stably localize to euchromatic interphase chromosome territories, but release upon disruption of the nuclear scaffold. Overall, findings suggest that instead of “tethering” chromosomal RNAs to the scaffold, SAF-A is one component of a multi-component matrix/scaffold supporting interphase nuclear architecture. Results indicate that Cot-1 and XIST RNAs form integral components of this scaffold and are required to maintain the chromosomal association of SAF-A, substantially advancing understanding of how chromatin-associated RNAs contribute to nuclear structure.

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