Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2.
Actively transcribing eukaryotic RNA polymerase II is highly phosphorylated on its repetitive carboxyl-terminal domain. We have isolated a protein kinase that phosphorylates serine residues in this repetitive domain. A component of this kinase is cdc2, the product of a cell-cycle control gene previously shown to be a component of M-phase-promoting factor and M-phase-specific histone H1 kinase. This observation suggests a role for the cdc2 protein kinase in transcriptional regulation.
Cisek
L J
LJ
Howard Hughes Medical Institute, Johns Hopkins School of Medicine, Baltimore, Maryland 21205.
Corden
J L
JL
D000595:Amino Acid Sequence; D000818:Animals; D016203:CDC2 Protein Kinase; D002453:Cell Cycle; D005786:Gene Expression Regulation; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D012319:RNA Polymerase II / Q000378:metabolism*; D013045:Species Specificity; D014158:Transcription, Genetic
D010750:Phosphoproteins; D011494:Protein Kinases; C060137:carboxy-terminal domain kinase; D016203:CDC2 Protein Kinase; D012319:RNA Polymerase II