Academic literature on the topic 'RNA polymerase II C-terminal domain'

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Journal articles on the topic "RNA polymerase II C-terminal domain"

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Dubois, Marie-Françoise, François Bonnet, Céline Cass, Van Trung Nguyen, Benoit Palancade, and Olivier Bensaude. "Modulation of RNA polymerase II C-terminal domain phosphorylation." Biochemistry and Cell Biology 77, no. 4 (1999): 392–93. http://dx.doi.org/10.1139/o99-903i.

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Stiller, J. W., and B. D. Hall. "Evolution of the RNA polymerase II C-terminal domain." Proceedings of the National Academy of Sciences 99, no. 9 (2002): 6091–96. http://dx.doi.org/10.1073/pnas.082646199.

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Abbas, Ata, Todd Romigh, and Charis Eng. "PTEN interacts with RNA polymerase II to dephosphorylate polymerase II C-terminal domain." Oncotarget 10, no. 48 (2019): 4951–59. http://dx.doi.org/10.18632/oncotarget.27128.

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Dahmus, Michael E. "Phosphorylation of the C-terminal domain of RNA polymerase II." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1261, no. 2 (1995): 171–82. http://dx.doi.org/10.1016/0167-4781(94)00233-s.

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Sano, Motoaki, Manabu Shirai, Derrick J. Rossi, et al. "RNA polymerase II C-terminal domain kinases in heart failure." Journal of Cardiac Failure 9, no. 5 (2003): S4. http://dx.doi.org/10.1016/s1071-9164(03)00165-9.

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García, Alicia, Emanuel Rosonina, James L. Manley, and Olga Calvo. "Sub1 Globally Regulates RNA Polymerase II C-Terminal Domain Phosphorylation." Molecular and Cellular Biology 30, no. 21 (2010): 5180–93. http://dx.doi.org/10.1128/mcb.00819-10.

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ABSTRACT The transcriptional coactivator Sub1 has been implicated in several aspects of mRNA metabolism in yeast, such as activation of transcription, termination, and 3′-end formation. Here, we present evidence that Sub1 plays a significant role in controlling phosphorylation of the RNA polymerase II large subunit C-terminal domain (CTD). We show that SUB1 genetically interacts with the genes encoding all four known CTD kinases, SRB10, KIN28, BUR1, and CTK1, suggesting that Sub1 acts to influence CTD phosphorylation at more than one step of the transcription cycle. To address this directly, w
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Bensaude, Olivier, François Bonnet, Céline Cassé, Marie-Françoise Dubois, Van Trung Nguyen, and Benoit Palancade. "Regulated phosphorylation of the RNA polymerase II C-terminal domain (CTD)." Biochemistry and Cell Biology 77, no. 4 (1999): 249–55. http://dx.doi.org/10.1139/o99-047.

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The largest subunit of RNA polymerase II has an intriguing feature in its carboxyl-terminal domain (CTD) that consists of multiple repeats of an evolutionary conserved motif of seven amino acids. CTD phosphorylation plays a pivotal role in controlling mRNA synthesis and maturation. In exponentially growing cells, the phosphate turnover on the CTD is fast; it is blocked by common inhibitors of transcription, such as 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole and actinomycin D. Transcription-independent changes in CTD phosphorylation are observed at critical developmental stages, such as m
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Dahmus, Michael E. "Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase II." Journal of Biological Chemistry 271, no. 32 (1996): 19009–12. http://dx.doi.org/10.1074/jbc.271.32.19009.

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O'Brien, Thomas, Steven Hardin, Arno Greenleaf, and John T. Lis. "Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation." Nature 370, no. 6484 (1994): 75–77. http://dx.doi.org/10.1038/370075a0.

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Gerber, Hans-Peter, Michael Hagmann, Katja Seipel, et al. "RNA polymerase II C-terminal domain required for enhancer-driven transcription." Nature 374, no. 6523 (1995): 660–62. http://dx.doi.org/10.1038/374660a0.

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Dissertations / Theses on the topic "RNA polymerase II C-terminal domain"

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Kobor, Michael S. "RNA polymerase II carboxy-terminal domain phosphatase." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ59023.pdf.

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Chapman, Rob. "A Functional Analysis of the RNA Polymerase II Large Subunit C-Terminal Domain." Diss., lmu, 2003. http://nbn-resolving.de/urn:nbn:de:bvb:19-11049.

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Kuznetsova, Olga. "Regulation of human RNA polymerase II CTD modifications." Thesis, University of Oxford, 2015. http://ora.ox.ac.uk/objects/uuid:e745b5b6-8a4a-4b7a-81d7-499bca8bfea1.

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Transcription of human protein-coding genes and most small nuclear RNA genes is mediated by RNA Polymerase II (Pol II). During a cycle of transcription, Pol II recruits a variety of factors that facilitate transcription elongation, RNA processing and termination, through its long, unstructured C-terminal domain (CTD). The CTD in humans comprises 52 tandem heptapeptide repeats with the consensus sequence Y<sub>1</sub>S<sub>2</sub>P<sub>3</sub>T<sub>4</sub>S<sub>5</sub>P<sub>6</sub>S<sub>7</sub>. Each amino acid of the heptapeptide can be chemically modified, which influences the recruitment of
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Boeing, Stefan. "Functions of Mediator and the RNA Polymerase II C-terminal Domain in Transcription Initiation." Diss., lmu, 2008. http://nbn-resolving.de/urn:nbn:de:bvb:19-97050.

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Soegaard, Teit Max Moscote. "The RNA polymerase II C-terminal domain : its phosphorylation and interaction with the mediator complex." Thesis, University College London (University of London), 2006. http://discovery.ucl.ac.uk/1445856/.

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The submitted thesis describes a biochemical investigation within the field of gene transcription. In yeast (Saccharomyces cerevisiae ) and the metazoans, the conserved RNA polymerase II (RNAPTJ) protein complex carries out regulated transcription. The C-terminal domain (CTD) of Rpbl (the largest subunit of RNAPII) consists of 26 hepta-peptide (YSPTSPS) repeats that are targeted by specific CTD-kinases and - phosphatases to change the phosphorylation of Ser2 and Ser5 resulting in two electrophoretically different forms of RNAPII - a fast migrating hypo-phosphorylated form and a slower migratin
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Chapman, Rob. "A functional analysis of the RNA polymerase II large subunit carboxy-terminal domain." [S.l.] : [s.n.], 2003. http://edoc.ub.uni-muenchen.de/archive/00001104.

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Roether, Susanne. "Functional Analysis of the RNA Polymerase II C-terminal Domain Kinase Ctk1 in the Yeast Saccharomyces cerevisiae." Diss., lmu, 2007. http://nbn-resolving.de/urn:nbn:de:bvb:19-73014.

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Schreieck, Amelie. "Role of the RNA polymerase II C-terminal domain in transcription termination and function of Spt5 in 3' RNA-processing factor recruitment." Diss., Ludwig-Maximilians-Universität München, 2013. http://nbn-resolving.de/urn:nbn:de:bvb:19-164544.

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Protein-coding genes in eukaryotes are transcribed by RNA polymerase II (Pol II). This process is tightly regulated and coupled to RNA processing. Many transcription and RNA processing factors are recruited to Pol II via its conserved C-terminal domain (CTD) containing 27 heptapeptide repeats of the consensus sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 in Saccharomyces cerevisiae. These repeats can be differentially phosphorylated during the transcription cycle serving as a code for interacting factors. During transcription initiation, Ser5 is phosphorylated at the 5’-end of genes and this pho
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Gu, Bo. "Co-transcriptional processing of pre-mRNA : Effects of RNA polymerase II carboxyl-terminal domain modification." Paris 6, 2012. http://www.theses.fr/2012PA066202.

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La transcription par l’ARN polymerase II (RNAPII) est un processus complexe qui inclue initiation, échappement du promoteur, elongation et terminaison. Chaque étape est régulée par un grand nombre d’éléments en cis et de facteurs en trans. La maturation des transcrits est aussi une succession d’étapes incluant la formation d’une coiffe en 5’, épissage puis clivage suivi de polyadénylation en 3’. Il est couramment admis que la transcription par la RNAPII et la maturation des transcrits est largement couplée et que les différents processus s’influencent mutuellement. En recherchant des ARNs non-
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Schreieck, Amelie [Verfasser], and Patrick [Akademischer Betreuer] Cramer. "Role of the RNA polymerase II C-terminal domain in transcription termination and function of Spt5 in 3' RNA-processing factor recruitment / Amelie Schreieck. Betreuer: Patrick Cramer." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2013. http://d-nb.info/1046503308/34.

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Books on the topic "RNA polymerase II C-terminal domain"

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Paraiso, Jean Paul. The role of the hyperphosphorylated carboxy-terminal domain of RNA polymerase II in transcription and pre-mRNA processing. National Library of Canada, 2002.

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Kobor, Michael S. RNA polymerase II carboxy-terminal domain phosphatase. 2001.

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Book chapters on the topic "RNA polymerase II C-terminal domain"

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KOIWA, HISASHI. "Phosphorylation of RNA polymerase II C-terminal domain and plant osmotic-stress responses." In Abiotic stress tolerance in plants. Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4389-9_3.

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Kang, Mona E., and Michael E. Dahmus. "The Unique C-Terminal Domain of RNA Polymerase II and Its Role in Transcription." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123171.ch2.

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Bensaude, O., M. F. Dubois, V. Legagneux, V. T. Nguyen, M. Pinto, and M. Morange. "Early Effects of Heat Shock on Enzymes: Heat Denaturation of Reporter Proteins and Activation of a Protein Kinase which Phosphorylates the C-terminal Domain of RNA Polymerase II." In Heat Shock. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76679-4_10.

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Lin, Patrick S., and Michael E. Dahmus. "Dephosphorylation of the Carboxyl-Terminal Domain of RNA Polymerase II." In Methods in Enzymology. Elsevier, 2003. http://dx.doi.org/10.1016/s0076-6879(03)70013-5.

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Jcisek, Lars, and Jeffry Lcorden. "[24] Purification of protein kinases that phosphorylate the repetitive carboxyl-terminal domain of eukaryotic RNA polymerase II." In Methods in Enzymology. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)00148-p.

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Hoheisel, Susanne, Michael S. Kobor, Erik Pierstorff, Jack Greenblatt, and Caroline M. Kane. "Purification and Assay of Saccharomyces cerevisiae Phosphatase That Acts on the C-Terminal Domain of the Largest Subunit of RNA Polymerase II." In Methods in Enzymology. Elsevier, 2003. http://dx.doi.org/10.1016/s0076-6879(03)70034-2.

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