Yeast TFIIH that is active in transcription can be dissociated into three components: a 5-subunit core, the SSL2 gene product, and a complex of 47 kDa, 45 kDa, and 33 kDa polypeptides that possesses protein kinase activity directed towards the C-terminal repeat domain of RNA polymerase II. These three components can reconstitute fully functional TFIIH, and all three are required for transcription in vitro. By contrast, TFIIH that is highly active in nucleotide excision repair (NER) lacks the kinase complex and instead contains the products of all other genes known to be required for NER in yeast: RAD1, RAD2, RAD4, RAD10, and RAD14. This repairosome is not active in reconstituted transcription in vitro and is significantly more active than any of the constituent polypeptides in correcting defective repair in extracts from strains mutated in NER genes.
|Number of pages||8|
|State||Published - Jan 13 1995|
Bibliographical noteFunding Information:
R. D. K. is the corresponding author for this study. We thank L. Prakash for anti-RAD14 antibodies and S. Bj6rklund and J. LaPointe for purified transcription factors. J, Q. S. was supported by a fellowship from the Danish Medical Research Council. W, J. F. was supported by a Medical Research Council of Canada Studentship. This work was supported by National Institutes of Health grants GM36659 to R. D. K., GM32263 to T. F. D., and CA12428 to E. C. F.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology (all)