Cdk-activating kinase complex is a component of human transcription factor TFIIH
Article Abstract:
Purification of transcription factor IIH (TFIIH) using chromatography reveals the presence of Cdk-activating kinase (Cak) complex in TFIIH. TFIIH-dependent transcription is blocked by affinity-purified antibodies against the Cak component cyclin H. Phosphorylation of the carboxy-terminal domain (CTI) is inhibited by antibodies of the Cak components, cyclin H and Cdk7. TFIIH phosphorylates both Cdc2 and Cdk2, implying a correlation between cell cycle control and transcription.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Interaction between an acidic activator and transcription factor TFIIB is required for transcriptional activation
Article Abstract:
The function of the TFIIB assembly in the mechanism which enhances acidic activator reactions was studied by designing acidic-activation-defective TFIIB mutants. Results supported the hypothesis that TFIIB mutants which were unable to react with acidic activators were also unable to stimulate the transcription process. Hence, the association of an acidic activator and TFIIB was required for the initiation of the transcription process.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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TFIIH is negatively regulated by cdk8-containing mediator complexes
Article Abstract:
Cdk7/cyclin C is found to control transcription by targeting cdk7/cyclin H subunits if initiation factor IIH.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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