Interacting partners of the Tfb2 subunit from yeast TFIIH

Denis E. Kainov, Luke A. Selth, Jesper Q. Svejstrup, Jean Marc Egly, Arnaud Poterzsman

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


TFIIH is an evolutionary conserved eukaryotic multi-protein complex composed of ten subunits. It is involved in transcription, cell cycle regulation, RNA splicing and the nucleotide excision DNA repair pathway (NER). Depending on the process in which it is functioning, the composition of TFIIH varies and activities of its subunits are differentially regulated. Here we focused on interplay between the Ssl2, Tfb2 and Tfb5 subunits of TFIIH from Saccharomyces cerevisiae. We found that Tfb2 bridges the Ssl2 helicase and the NER-specific Tfb5 subunit. Moreover, the Tfb5-interacting domain of Tfb2 also binds nucleic acids (NA), although the addition of Tfb5 triggers dissociation of NA from Tfb2. In yeast cells, deletion of TFB5 is more detrimental to NER than loss of the Tfb5/NA-interacting domain of Tfb2, while combining these mutations resulted in suppression of the UV sensitivity of tfb5Δ. The implications of our findings in regards to TFIIH function and group A trichothiodystrophy, an inherited disease associated with mutations in the human TFB5 gene, are discussed.

Original languageEnglish
Pages (from-to)33-39
Number of pages7
JournalDNA Repair
Issue number1
Publication statusPublished - 2 Jan 2010
Externally publishedYes


  • NER
  • Transcription
  • TTD-A


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