J 2013

The CTD code of RNA polymerase II: a structural view

JASNOVIDOVA, Olga and Richard ŠTEFL

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

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

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
Name: CEITEC - central european institute of technology
GAP305/10/1490, research and development project
Name: Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu
Investor: Czech Science Foundation
GBP305/12/G034, research and development project
Name: Centrum biologie RNA