| The RNA polymerase II CTD coordinates transcription and RNA processing. | |
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MedLine Citation:
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PMID: 23028141 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The C-terminal domain (CTD) of the RNA polymerase II largest subunit consists of multiple heptad repeats (consensus Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7), varying in number from 26 in yeast to 52 in vertebrates. The CTD functions to help couple transcription and processing of the nascent RNA and also plays roles in transcription elongation and termination. The CTD is subject to extensive post-translational modification, most notably phosphorylation, during the transcription cycle, which modulates its activities in the above processes. Therefore, understanding the nature of CTD modifications, including how they function and how they are regulated, is essential to understanding the mechanisms that control gene expression. While the significance of phosphorylation of Ser2 and Ser5 residues has been studied and appreciated for some time, several additional modifications have more recently been added to the CTD repertoire, and insight into their function has begun to emerge. Here, we review findings regarding modification and function of the CTD, highlighting the important role this unique domain plays in coordinating gene activity. |
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Authors:
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Jing-Ping Hsin; James L Manley |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Review |
Journal Detail:
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Title: Genes & development Volume: 26 ISSN: 1549-5477 ISO Abbreviation: Genes Dev. Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-02 Completed Date: 2012-12-05 Revised Date: 2013-05-20 |
Medline Journal Info:
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Nlm Unique ID: 8711660 Medline TA: Genes Dev Country: United States |
Other Details:
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Languages: eng Pagination: 2119-37 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, Columbia University, New York, New York 10027, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Chromatin / genetics, metabolism Humans Phosphoprotein Phosphatases / metabolism Protein Kinases / metabolism Protein Structure, Tertiary RNA Polymerase II / metabolism* RNA Processing, Post-Transcriptional / physiology* Transcription, Genetic / physiology* |
| Grant Support | |
ID/Acronym/Agency:
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R01 GM048259/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Chromatin; EC 2.7.-/Protein Kinases; EC 2.7.1.-/carboxy-terminal domain kinase; EC 2.7.7.-/RNA Polymerase II; EC 3.1.3.16/Phosphoprotein Phosphatases; EC 3.1.3.16/carboxy-terminal domain phosphatase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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