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.