The CTD code of RNA polymerase II: a structural view
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
23042580
DOI
10.1002/wrna.1138
Knihovny.cz E-resources
- MeSH
- Transcription, Genetic MeSH
- Methyltransferases metabolism MeSH
- NIMA-Interacting Peptidylprolyl Isomerase MeSH
- Peptidylprolyl Isomerase metabolism MeSH
- Protein Processing, Post-Translational * MeSH
- Proline metabolism MeSH
- Phosphoprotein Phosphatases MeSH
- RNA-Binding Proteins genetics metabolism MeSH
- RNA Polymerase II * chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae Proteins MeSH
- Saccharomyces cerevisiae enzymology genetics MeSH
- Amino Acid Sequence MeSH
- Protein Structure, Tertiary MeSH
- Carrier Proteins metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- ESS1 protein, S cerevisiae MeSH Browser
- Methyltransferases MeSH
- mRNA (nucleoside-O(2'))-methyltransferase MeSH Browser
- NIMA-Interacting Peptidylprolyl Isomerase MeSH
- Peptidylprolyl Isomerase MeSH
- PIN1 protein, human MeSH Browser
- Proline MeSH
- Phosphoprotein Phosphatases MeSH
- RNA-Binding Proteins MeSH
- RNA Polymerase II * MeSH
- Saccharomyces cerevisiae Proteins MeSH
- SSU72 protein, human MeSH Browser
- Carrier Proteins MeSH
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 Y(1)S(2)P(3) T(4)S(5)P(6)S(7). 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 CTD modifications 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.
References provided by Crossref.org
Sequence and structural determinants of RNAPII CTD phase-separation and phosphorylation by CDK7
Yeast Spt6 Reads Multiple Phosphorylation Patterns of RNA Polymerase II C-Terminal Domain In Vitro
Structure and dynamics of the RNAPII CTDsome with Rtt103
Molecular basis for coordinating transcription termination with noncoding RNA degradation
Structure and semi-sequence-specific RNA binding of Nrd1