The Ser7 phosphorylation of RNA polymerase II-CTD is required for the recruitment of E3 ubiquitin ligase Asr1 and subtelomeric gene silencing.

ABSTRACT: The carboxy terminal domain (CTD) of the largest subunit of RNA polymerase II (RNAPII) is composed of a tandem heptad sequence of Tyr1Ser2Pro3Thr4Ser5Pro6Ser7, which helps facilitate the transcription of all mRNA and the majority of noncoding RNA. The serines of RNAPII-CTD undergo differential phosphorylation, with Ser5 phosphorylation being predominant at the 5' end, Ser2 phosphorylation toward the 3' end, and Ser7 phosphorylation (Ser7P) present throughout the ORF during transcription. The phosphorylation of Ser2 and Ser5 coordinates the recruitment of proteins involved in the progression of transcription. The Ser7P has been shown to play a role in the processing and termination of small nuclear RNA transcription in both budding yeast and humans. Nevertheless, the effect of this phosphor

SUBMITTER: Sudarshan N 

PROVIDER: S-EPMC12270679 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature