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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 and Richard ŠTEFL. The CTD code of RNA polymerase II: a structural view. \textit{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.
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