Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair

William J. Feaver, Jesper Q. Svejstrup, Lee Bardwell, A. Jane Bardwell, Stephen Buratowski, Keith D. Gulyas, Thomas F. Donahue, Errol C. Friedberg, Roger D. Kornberg

Research output: Contribution to journalArticlepeer-review

41 Scopus citations


Yeast RNA polymerase II initiation factor b, homolog of human TFIIH, is a protein kinase capable of phosphorylating the C-terminal repeat domain of the polymerase; it possesses a DNA-dependent ATPase activity as well. The 85 kd and 50 kd subunits of factor b are now identified as RAD3 and SSL1 proteins, respectively; both are known to be involved in DNA repair. Factor b interacts specifically with another DNA repair protein, SSL2. The ATPase activity of factor b may be due entirely to that associated with a helicase function of RAD3. Factor b transcriptional activity was unaffected, however, by amino acid substitution at a conserved residue in the RAD3 nucleotide-binding domain, suggesting that the ATPase/helicase function is not required for transcription. These results identify factor b as a core repairosome, which may be responsible for the preferential repair of actively transcribed genes in eukaryotes.

Original languageEnglish (US)
Pages (from-to)1379-1387
Number of pages9
Issue number7
StatePublished - Dec 31 1993

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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