JASNOVIDOVA, Olga and Richard ŠTEFL. The CTD code of RNA polymerase II: a structural view. Online. Wiley Interdisciplinary Reviews: RNA. Hoboken, USA: WILEY-BLACKWELL, 2013, vol. 4, No 1, p. 1-16. ISSN 1757-7004. Available from: https://dx.doi.org/10.1002/wrna.1138. [citováno 2024-04-24]
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Basic information
Original name The CTD code of RNA polymerase II: a structural view
Authors JASNOVIDOVA, Olga (233 Estonia, belonging to the institution) and Richard ŠTEFL (203 Czech Republic, guarantor, belonging to the institution)
Edition Wiley Interdisciplinary Reviews: RNA, Hoboken, USA, WILEY-BLACKWELL, 2013, 1757-7004.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 6.154
RIV identification code RIV/00216224:14740/13:00065946
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1002/wrna.1138
UT WoS 000312735800001
Keywords in English CARBOXYL-TERMINAL DOMAIN; PROLYL CIS/TRANS ISOMERASES; MESSENGER-RNA; TRANSCRIPTION TERMINATION; GENE-EXPRESSION; CAPPING ENZYME; O-GLCNAC; TYROSINE PHOSPHORYLATION; PERVASIVE TRANSCRIPTION; BIDIRECTIONAL PROMOTERS
Tags ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 24/10/2013 09:04.
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 CTDmodifications 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
Links
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
GAP305/10/1490, research and development projectName: Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu
Investor: Czech Science Foundation
GBP305/12/G034, research and development projectName: Centrum biologie RNA
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