The CTD code of RNA polymerase II: a structural view

Investor logo
Investor logo
Investor logo

Warning

This publication doesn't include Faculty of Education. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

JASNOVIDOVA Olga ŠTEFL Richard

Year of publication 2013
Type Article in Periodical
Magazine / Source Wiley Interdisciplinary Reviews: RNA
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.ncbi.nlm.nih.gov/pubmed/23042580
Doi http://dx.doi.org/10.1002/wrna.1138
Field Biochemistry
Keywords CARBOXYL-TERMINAL DOMAIN; PROLYL CIS/TRANS ISOMERASES; MESSENGER-RNA; TRANSCRIPTION TERMINATION; GENE-EXPRESSION; CAPPING ENZYME; O-GLCNAC; TYROSINE PHOSPHORYLATION; PERVASIVE TRANSCRIPTION; BIDIRECTIONAL PROMOTERS
Description 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
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.