The Mo15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor.
January 1994
Article
volume 79, issue 6 pp 1093-1101.
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A protein kinase activity that phosphorylates the C-terminal domain (CTD) of RNA polymerase II and is associated with the basal transcription-repair factor TFIIH (also called BTF2) resides with MO15, a cyclin-dependent protein kinase that was first found to be involved in cell cycle regulation. Using in vivo and in vitro repair assays, we show that MO15 is important for nucleotide excision repair, most likely through its association with TFIIH, thus providing an unexpected link among three important cellular mechanisms.
Keywords
- Comparative Study
- Human
- Support, Non-U.S. Gov't
- *DNA Repair
- Protein Binding
- Amino Acid Sequence
- Molecular Sequence Data
- *Transcription, Genetic
- Cell Nucleus/metabolism
- Phosphorylation
- *Transcription Factors, TFII
- 0 (Taf6 protein, Drosophila)
- 0 (Transcription Factors)
- 0 (Transcription Factors, TFII)
- 148710-81-0 (transcription factor TFIIH)
- 0 (Peptide Fragments)
- EC 2.7.7.- (RNA Polymerase II)
- RNA Polymerase II/metabolism
- *Cyclin-Dependent Kinases
- Cell Cycle/*physiology
- EC 2.7.1.37 (Cyclin-Dependent Kinases)
- EC 2.7.1.37 (Protein-Serine-Threonine Kinases)
- EC 2.7.1.37 (cyclin-dependent kinase-activating kinase)
- Peptide Fragments/metabolism
- Protein-Serine-Threonine Kinases/immunology/isolation & purification/*metabolism
- Transcription Factors/immunology/isolation & purification/*metabolism
Automatically Extracted Terms
- mo 15
- tfiih
- kinase
- transcription
- activity
- fraction
- rna pol ii
- figure
- repair
- factor
- antibody
- subunit
- mo 1 5
- protein
- phosphorylation
- assay
- rna polymerase ii
- gradient
- dna repair
- tfiih subunits
