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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair. Feaver, W.J., Svejstrup, J.Q., Bardwell, L., Bardwell, A.J., Buratowski, S., Gulyas, K.D., Donahue, T.F., Friedberg, E.C., Kornberg, R.D. Cell (1993) [Pubmed]
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