TY - JOUR

T1 - Interacting partners of the Tfb2 subunit from yeast TFIIH

AU - Kainov, Denis E.

AU - Selth, Luke A.

AU - Svejstrup, Jesper Q.

AU - Egly, Jean Marc

AU - Poterzsman, Arnaud

N1 - Funding Information: This work was supported by a generous in-house grant to J.Q.S., an ERC advance personal grant 2009 to J.M.E as well as INCA (INCA-2008-041) and ANR (ANR-08-042-02) funding for A.P. and J.M.E., D.E.K. and L.A. were supported by EMBO long-term fellowships.

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

KW - NER

KW - TFIIH

KW - Transcription

KW - TTD-A

U2 - 10.1016/j.dnarep.2009.10.002

DO - 10.1016/j.dnarep.2009.10.002

M3 - Journal article

C2 - 19897425

AN - SCOPUS:73149083941

VL - 9

SP - 33

EP - 39

JO - DNA Repair

JF - DNA Repair

SN - 1568-7864

IS - 1

ER -