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@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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