Answers are grounded in this paper and cite their sources.
The cyclin T/CDK9 complex, also called positive transcription elongation factor b (P-TEFb) phosphorylates the C-terminal domain of the large fragment of the RNA polymerase II. This action is a hallmark of the transition from transcription initiation to elongation. P-TEFb is itself modified by phosphorylation and ubiquitination. Recently, the core components of P-TEFb, cyclin T1 and CDK9, were identified as novel substrates of histone acetyltransferases. Here, we review how posttranslational modifications regulate the activity of the P-TEFb complex and discuss how acetylation of the complex optimizes transcription elongation in the context of other posttranslational modifications.
No takes yet. Share an insight, caveat, or question.
Cho et al. (2010) studied this question.
Synapse has enriched 5 related papers. Consider them for comparative context: