Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
Autor: | Corinna Hintermair, Martin Heidemann, Kirsten Voß, Dirk Eick |
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Rok vydání: | 2012 |
Předmět: |
Transcription
Genetic Biophysics RNA polymerase II environment and public health Biochemistry Models Biological Structural Biology Transcription (biology) Genetics Consensus sequence Serine Animals Humans Amino Acid Sequence Phosphorylation Molecular Biology Gene RNA polymerase II holoenzyme biology Cell biology Protein Structure Tertiary enzymes and coenzymes (carbohydrates) Kinetics health occupations biology.protein CTD RNA Polymerase II Transcription factor II D Protein Kinases |
Zdroj: | Biochimica et biophysica acta. 1829(1) |
ISSN: | 0006-3002 |
Popis: | The eukaryotic RNA polymerase II (RNAPII) catalyzes the transcription of all protein encoding genes and is also responsible for the generation of small regulatory RNAs. RNAPII has evolved a unique domain composed of heptapeptide repeats with the consensus sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 at the C-terminus (CTD) of its largest subunit (Rpb1). Dynamic phosphorylation patterns of serine residues in CTD during gene transcription coordinate the recruitment of factors to the elongating RNAPII and to the nascent transcript. Recent studies identified threonine 4 and tyrosine 1 as new CTD modifications and thereby expanded the "CTD code". In this review, we focus on CTD phosphorylation and its function in the RNAPII transcription cycle. We also discuss in detail the limitations of the phosphospecific CTD antibodies, which are used in all studies. This article is part of a Special Issue entitled: RNA Polymerase II Transcript Elongation. |
Databáze: | OpenAIRE |
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