Cdk-activating kinase complex is a component of human transcription factor TFIIH.

Transcription factor IIH (TFIIH) contains a kinase capable of phosphorylating the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (RNAPII). Here we report the identification of the Cdk-activating kinase (Cak) complex (Cdk7 and cyclin H) as a component of TFIIH after extensive purification of TFIIH by chromatography. ...
We find that affinity-purified antibodies directed against cyclin H inhibit TFIIH-dependent transcription and that both cyclin H and Cdk7 antibodies inhibit phosphorylation of the CTD of the largest subunit of the RNAPII in the preinitiation complex. Cak is present in at least two distinct complexes, TFIIH and a smaller complex that is unable to phosphorylate RNAPII in the preinitiation complex. Both Cak complexes, as well as recombinant Cak, phosphorylate a CTD peptide. Finally, TFIIH was shown to phosphorylate both Cdc2 and Cdk2, suggesting that there could be a link between transcription and the cell cycle machinery.
Mesh Terms:
Amino Acid Sequence, Chromatography, Affinity, Cyclin H, Cyclin-Dependent Kinases, Cyclins, Detergents, Hela Cells, Humans, Immunologic Techniques, Molecular Sequence Data, Phosphorylation, Protein Kinases, Protein-Serine-Threonine Kinases, RNA Polymerase II, Recombinant Proteins, Sarcosine, Transcription Factor TFIIH, Transcription Factors, Transcription Factors, TFII, Transcription, Genetic
Nature
Date: Mar. 16, 1995
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