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- Title
Modulation of TFIIH-associated kinase activity by complex formation and its relationship with CTD phosphorylation of RNA polymerase II.
- Authors
Watanabe, Y; Fujimoto, H; Watanabe, T; Maekawa, T; Masutani, C; Hanaoka, F; Ohkuma, Y
- Abstract
The general transcription factor TFIIH plays important roles in initiation and the transition to elongation steps of transcription by RNA polymerase II (PolII). Both roles are dependent on the protein kinase, DNA-dependent ATPase and DNA helicase activities of TFIIH. However, how these enzyme activities of TFIIH contribute to transcription has remained elusive. TFIIH consists of nine subunits, and one of them, Cdk7, possesses kinase activity. Here the substrate specificities of TFIIH and two forms of the Cdk7-containing kinase complex are compared, and the relationship between transcription activity and the TFIIH-dependent phosphorylation of the carboxy terminal domain of the largest subunit of PolII (CTD) is studied.
- Publication
Genes to cells : devoted to molecular & cellular mechanisms, 2000, Vol 5, Issue 5, p407
- ISSN
1356-9597
- Publication type
Journal Article
- DOI
10.1046/j.1365-2443.2000.00336.x