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Association of Cdk-activating kinase subunits with transcription factor TFIIH

Nature volume 374, pages 280–282 (1995)Cite this article

Abstract

THE RNA polymerase II large subunit contains an essential carboxy-terminal domain (CTD) believed to be involved in the response to regulators during transcription initiation1–10. The CTD is phosphorylated on a portion of RNA polymerase II molecules in in vivo11,12 and it can be phosphorylated by the general transcription factor TFIIH in vitro13–15. A highly purified TFIIH from rat liver has been described16; this, like human and yeast TFIIH, contains associated CTD kinase and helicase activities13–18. We report here that two polypeptides of the purified mammalian TFIIH are the MO15/Cdk7 kinase and cyclin H subunits of the Cdk-activating kinase Cak19–21, previously identified as a positive regulator of Cdc2 and Cdk2. TFIIH and Cak preparations are each capable of phosphorylating recombinant CTD and recombi-nant Cdk2 proteins. The presence of Cak in TFIIH indicates that Cak may have roles in transcriptional regulation and in cell-cycle control.

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Author notes

  1. Joan Weliky Conaway and Ronald C. Conaway: Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, USA

Authors and Affiliations

  1. Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, Massachusetts, 02142

    Hiroaki Serizawa, Tomi P. Mäkelä, Joan Weliky Conaway, Ronald C. Conaway, Robert A. Weinberg & Richard A. Young

  2. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Hiroaki Serizawa, Tomi P. Mäkelä, Joan Weliky Conaway, Ronald C. Conaway, Robert A. Weinberg & Richard A. Young

Authors
  1. Hiroaki Serizawa
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  2. Tomi P. Mäkelä
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  3. Joan Weliky Conaway
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  4. Ronald C. Conaway
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  5. Robert A. Weinberg
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  6. Richard A. Young
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Serizawa, H., Mäkelä, T., Conaway, J. et al. Association of Cdk-activating kinase subunits with transcription factor TFIIH. Nature 374, 280–282 (1995). https://doi.org/10.1038/374280a0

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