Regulated phosphorylation of the RNA polymerase II C-terminal domain (CTD).
The largest subunit of RNA polymerase II has an intriguing feature in its carboxyl-terminal domain (CTD) that consists of multiple repeats of an evolutionary conserved motif of seven amino acids. CTD phosphorylation plays a pivotal role in controlling mRNA synthesis and maturation. In exponentially growing cells, the phosphate turnover on the CTD is fast; it is blocked by common inhibitors of transcription, such as 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole and actinomycin D. Transcription-independent changes in CTD phosphorylation are observed at critical developmental stages, such as meiosis and early development.
Bensaude
O
O
Laboratoire de génétique moléculaire, Ecole normale supérieure, Paris, France. bensaude@wotan.ens.fr
Bonnet
F
F
Cassé
C
C
Dubois
M F
MF
Nguyen
V T
VT
Palancade
B
B
D000818:Animals; D006358:Hot Temperature; D006801:Humans; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D011487:Protein Conformation; D011494:Protein Kinases / Q000378:metabolism; D012319:RNA Polymerase II / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism
D012333:RNA, Messenger; D011494:Protein Kinases; C060137:carboxy-terminal domain kinase; D012319:RNA Polymerase II; D010749:Phosphoprotein Phosphatases; C116022:carboxy-terminal domain phosphatase