The CTD code of RNA polymerase II: a structural view

J 2013

The CTD code of RNA polymerase II: a structural view

JASNOVIDOVA, Olga a Richard ŠTEFL

Základní údaje

Originální název

The CTD code of RNA polymerase II: a structural view

Autoři

JASNOVIDOVA, Olga (233 Estonsko, domácí) a Richard ŠTEFL (203 Česká republika, garant, domácí)

Vydání

Wiley Interdisciplinary Reviews: RNA, Hoboken, USA, WILEY-BLACKWELL, 2013, 1757-7004

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 6.154

Kód RIV

RIV/00216224:14740/13:00065946

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1002/wrna.1138

UT WoS

000312735800001

Klíčová slova anglicky

CARBOXYL-TERMINAL DOMAIN; PROLYL CIS/TRANS ISOMERASES; MESSENGER-RNA; TRANSCRIPTION TERMINATION; GENE-EXPRESSION; CAPPING ENZYME; O-GLCNAC; TYROSINE PHOSPHORYLATION; PERVASIVE TRANSCRIPTION; BIDIRECTIONAL PROMOTERS

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 24. 10. 2013 09:04, Olga Křížová

Anotace

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

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GAP305/10/1490, projekt VaV

Název: Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu

Investor: Grantová agentura ČR, Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu

GBP305/12/G034, projekt VaV

Název: Centrum biologie RNA

Citovat

JASNOVIDOVA, Olga a Richard ŠTEFL. The CTD code of RNA polymerase II: a structural view. Wiley Interdisciplinary Reviews: RNA. Hoboken, USA: WILEY-BLACKWELL, 2013, roč. 4, č. 1, s. 1-16. ISSN 1757-7004. Dostupné z: https://dx.doi.org/10.1002/wrna.1138.

@article{1073506,
   author = {Jasnovidova, Olga and Štefl, Richard},
   article_location = {Hoboken, USA},
   article_number = {1},
   doi = {http://dx.doi.org/10.1002/wrna.1138},
   keywords = {CARBOXYL-TERMINAL DOMAIN; PROLYL CIS/TRANS ISOMERASES; MESSENGER-RNA; TRANSCRIPTION TERMINATION; GENE-EXPRESSION; CAPPING ENZYME; O-GLCNAC; TYROSINE PHOSPHORYLATION; PERVASIVE TRANSCRIPTION; BIDIRECTIONAL PROMOTERS},
   language = {eng},
   issn = {1757-7004},
   journal = {Wiley Interdisciplinary Reviews: RNA},
   title = {The CTD code of RNA polymerase II: a structural view},
   url = {http://www.ncbi.nlm.nih.gov/pubmed/23042580},
   volume = {4},
   year = {2013}
}

TY  - JOUR
ID  - 1073506
AU  - Jasnovidova, Olga - Štefl, Richard
PY  - 2013
TI  - The CTD code of RNA polymerase II: a structural view
JF  - Wiley Interdisciplinary Reviews: RNA
VL  - 4
IS  - 1
SP  - 1-16
EP  - 1-16
PB  - WILEY-BLACKWELL
SN  - 17577004
KW  - CARBOXYL-TERMINAL DOMAIN
KW  - PROLYL CIS/TRANS ISOMERASES
KW  - MESSENGER-RNA
KW  - TRANSCRIPTION TERMINATION
KW  - GENE-EXPRESSION
KW  - CAPPING ENZYME
KW  - O-GLCNAC
KW  - TYROSINE PHOSPHORYLATION
KW  - PERVASIVE TRANSCRIPTION
KW  - BIDIRECTIONAL PROMOTERS
UR  - http://www.ncbi.nlm.nih.gov/pubmed/23042580
L2  - http://www.ncbi.nlm.nih.gov/pubmed/23042580
N2  - 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
ER  -

JASNOVIDOVA, Olga a Richard ŠTEFL. The CTD code of RNA polymerase II: a structural view. \textit{Wiley Interdisciplinary Reviews: RNA}. Hoboken, USA: WILEY-BLACKWELL, 2013, roč.~4, č.~1, s.~1-16. ISSN~1757-7004. Dostupné z: https://dx.doi.org/10.1002/wrna.1138.

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