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The transcription/DNA repair factor TFIIH may be resolved into at least two subcomplexes: the core TFIIH and the cdk-activating kinase (CAK) complex. The CAK complex, which is also found free in the cell, is composed of cdk7, cyclin H, and MAT1. In the present work, we found that the C terminus of MAT1 binds to the cdk7 x cyclin H complex and activates the cdk7 kinase activity. The median portion of MAT1, which contains a coiled-coil motif, allows the binding of CAK to the TFIIH core through interactions with both XPD and XPB helicases. Furthermore, using recombinant TFIIH complexes, it is demonstrated that the N-terminal RING finger domain of MAT1 is crucial for transcription activation and participates to the phosphorylation of the C-terminal domain of the largest subunit of the RNA polymerase II.

Original publication

DOI

10.1074/jbc.M002578200

Type

Journal article

Journal

J Biol Chem

Publication Date

28/07/2000

Volume

275

Pages

22815 - 22823

Keywords

Amino Acid Sequence, Animals, Cell Line, Cyclin H, Cyclin-Dependent Kinases, Cyclins, DNA Helicases, Gene Expression Regulation, Enzymologic, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein-Serine-Threonine Kinases, Recombinant Proteins, Spodoptera, Substrate Specificity, Transcription Factor TFIIH, Transcription Factors, Transcription Factors, TFII, Transcription, Genetic