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The CTD code of RNA polymerase II: a structural view

The CTD code of RNA polymerase II: a structural view RNA polymerase II (RNA pol II) is not only the fundamental enzyme for gene expression but also the central coordinator of co‐transcriptional processing. RNA pol II associates with a large number of enzymes and protein/RNA‐binding factors through its C‐terminal domain (CTD) that consists of tandem repeats of the heptapeptide consensus Y1S2P3T4S5P6S7. The CTD is posttranslationally modified, yielding specific patterns (often called the CTD code) that are recognized by appropriate factors in coordination with the transcription cycle. Serine phosphorylations are currently the best characterized elements of the CTD code; however, the roles of the proline isomerization and other modifications of the CTD remain poorly understood. The dynamic remodeling of the CTD modifications by kinases, phosphatases, isomerases, and other enzymes introduce changes in the CTD structure and dynamics. These changes serve as structural switches that spatially and temporally regulate the binding of processing factors. Recent structural studies of the CTD bound to various proteins have revealed the basic rules that govern the recognition of these switches and shed light on the roles of these protein factors in the assemblies of the processing machineries. WIREs RNA 2013, 4:1–16. doi: 10.1002/wrna.1138 For further resources related to this article, please visit the WIREs website. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Wiley Interdisciplinary Reviews: Rna Wiley

The CTD code of RNA polymerase II: a structural view

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References (111)

Publisher
Wiley
Copyright
Copyright © 2012 John Wiley & Sons, Ltd.
ISSN
1757-7004
eISSN
1757-7012
DOI
10.1002/wrna.1138
pmid
23042580
Publisher site
See Article on Publisher Site

Abstract

RNA polymerase II (RNA pol II) is not only the fundamental enzyme for gene expression but also the central coordinator of co‐transcriptional processing. RNA pol II associates with a large number of enzymes and protein/RNA‐binding factors through its C‐terminal domain (CTD) that consists of tandem repeats of the heptapeptide consensus Y1S2P3T4S5P6S7. The CTD is posttranslationally modified, yielding specific patterns (often called the CTD code) that are recognized by appropriate factors in coordination with the transcription cycle. Serine phosphorylations are currently the best characterized elements of the CTD code; however, the roles of the proline isomerization and other modifications of the CTD remain poorly understood. The dynamic remodeling of the CTD modifications by kinases, phosphatases, isomerases, and other enzymes introduce changes in the CTD structure and dynamics. These changes serve as structural switches that spatially and temporally regulate the binding of processing factors. Recent structural studies of the CTD bound to various proteins have revealed the basic rules that govern the recognition of these switches and shed light on the roles of these protein factors in the assemblies of the processing machineries. WIREs RNA 2013, 4:1–16. doi: 10.1002/wrna.1138 For further resources related to this article, please visit the WIREs website.

Journal

Wiley Interdisciplinary Reviews: RnaWiley

Published: Jan 1, 2013

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