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

Ramin Shiekhattar, Fred Mermelstein, Robert P. Fisher, Ronny Drapkin, Dynlacht Brian, Holly C. Wessling, David O. Morgan, Danny Reinberg

Research output: Contribution to journalArticlepeer-review

344 Scopus citations

Abstract

TRANSCRIPTION factor IIH (TFIIH) contains a kinase capable of phosphorylating the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (RNAPII)1–3. 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.

Original languageEnglish (US)
Pages (from-to)283-287
Number of pages5
JournalNature
Volume374
Issue number6519
DOIs
StatePublished - Mar 16 1995
Externally publishedYes

ASJC Scopus subject areas

  • General

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