The molecular mechanism of mitotic inhibition of TFIIH is mediated by phosphorylation of CDK7
AUTOR(ES)
Akoulitchev, Sasha
FONTE
Cold Spring Harbor Laboratory Press
RESUMO
TFIIH is a multisubunit complex, containing ATPase, helicases, and kinase activities. Functionally, TFIIH has been implicated in transcription by RNA polymerase II (RNAPII) and in nucleotide excision repair. A member of the cyclin-dependent kinase family, CDK7, is the kinase subunit of TFIIH. Genetically, CDK7 homologues have been implicated in transcription in Saccharomyces cerevisiae, and in mitotic regulation in Schizosaccharomyces pombe. Here we show that in mitosis the CDK7 subunit of TFIIH and the largest subunit of RNAPII become hyperphosphorylated. MPF-induced phosphorylation of CDK7 results in inhibition of the TFIIH-associated kinase and transcription activities. Negative and positive regulation of TFIIH requires phosphorylation within the T-loop of CDK7. Our data establishes TFIIH and its subunit CDK7 as a direct link between the regulation of transcription and the cell cycle.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=317239Documentos Relacionados
- Repression of TFIIH Transcriptional Activity and TFIIH-Associated cdk7 Kinase Activity at Mitosis
- MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH.
- Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity
- Cdk7 Is Required for Full Activation of Drosophila Heat Shock Genes and RNA Polymerase II Phosphorylation In Vivo
- The Histidine Triad Protein Hint Is Not Required for Murine Development or Cdk7 Function