PTEN interacts with RNA polymerase II to dephosphorylate polymerase II C-terminal domain

Functions of Mediator and the RNA Polymerase II C-terminal Domain in TranscriptiFunctions of Mediator and the RNA Polymerase II C-terminal Domain in Transcription Initiation

A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II.

The largest subunit of RNA polymerase II shows a striking difference in the degree of phosphorylation, depending on its functional state: initiating and elongating polymerases are unphosphorylated and highly phosphorylated respectively. Phosphorylation mostly occurs at the C-terminal domain (CTD), which consists of a repetitive heptapeptide structure. Using the yeast two-hybrid system, we have ...

Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain

The carboxy-terminal domain (CTD) of the RNA polymerase II (Pol II) large subunit cycles through phosphorylation states that correlate with progression through the transcription cycle and regulate nascent mRNA processing. Structural analyses of yeast and mammalian CTD are hampered by their repetitive sequences. Here we identify a region of the Drosophila melanogaster CTD that is essential for P...

Structural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain

RNA polymerase II contains a repetitive, intrinsically disordered, C-terminal domain (CTD) composed of heptads of the consensus sequence YSPTSPS. The CTD is heavily phosphorylated and serves as a scaffold, interacting with factors involved in transcription initiation, elongation and termination, RNA processing and chromatin modification. Despite being a nexus of eukaryotic gene regulation, the ...

RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7

The synthesis of mRNA by Pol II involves cotranscriptional premRNA processing including 5′ capping, splicing and 3′-end processing. Pol II recruits pre-mRNA–processing factors via its CTD throughout transcription1–3, and this process is regulated by changes in CTD phosphorylation4. The CTD forms a flexible extension of Pol II consisting of 26 (yeast) or 52 (human) heptapeptide repeats of the co...