Updating the rna polymerase ctd
Speaker: Dr Shona Murphy Reader in Molecular Biology, Personnel Administrator and Academic Bursar, Oxford University Our research aims to elucidate the mechanisms underlying control of gene expression at the levels of transcription and co-transcriptional RNA processing, focusing recently on the role of co-transcriptional modification of the carboxyl-terminal domain (CTD) of RNA polymerase II. We are using the human genes for the U1 and U2 small nuclear (sn)RNAs involved in splicing as model gene systems to study the coupling between dynamic CTD phosphorylation and gene expression. Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9.
Protein binding generally increases upon phosphorylation of the CTD, and 3?-end processing is stimulated in vitro by phosphorylated CTD.DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and m RNA processing.Acts as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.
Pol II is the central component of the basal RNA polymerase II transcription machinery.