Detailed Information on Publication Record
2013
The CTD code of RNA polymerase II: a structural view
JASNOVIDOVA, Olga and Richard ŠTEFLBasic 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
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 6.154
RIV identification code
RIV/00216224:14740/13:00065946
Organization unit
Central European Institute of Technology
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
International impact, Reviewed
Změněno: 24/10/2013 09:04, Olga Křížová
Abstract
V originále
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 project |
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GAP305/10/1490, research and development project |
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GBP305/12/G034, research and development project |
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