Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Molecular Biology Année : 2007

Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy.

Résumé

Trichothiodystrophy (TTD) is a rare hereditary multi-system disorder associated with defects in nucleotide excision repair (NER) and transcription as consequences of mutations in XPB, XPD and p8/TTD-A subunits of transcription factor IIH (TFIIH). Here, we report the solution structure of the p8/TTD-A protein, a small alpha/beta protein built around an antiparallel beta-sheet that forms a homodimer with an extended interface. In order to characterize the dimer interface, we have introduced a mutation at position 44, which destabilizes the dimeric form of the protein. We have shown that this mutation has no effect on the intrinsic ability of p8/TTD-A to stimulate NER in vitro, but affects the capacity of p8/TTD-A to restore TFIIH concentration in TTD-A fibroblasts. Point mutations found in TTD-A patients are discussed on the basis of the present structure.

Dates et versions

hal-00190943 , version 1 (23-11-2007)

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Citer

Marc Vitorino, Frédéric Coin, Olga Zlobinskaya, Robert Andrew Atkinson, Dino Moras, et al.. Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy.. Journal of Molecular Biology, 2007, 368 (2), pp.473-80. ⟨10.1016/j.jmb.2007.02.020⟩. ⟨hal-00190943⟩
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