Structural characterization of the cysteine-rich domain of TFIIH p44 subunit.
Fiche publication
Date publication
octobre 2000
Auteurs
Membres identifiés du Cancéropôle Est :
Dr KIEFFER Bruno, Dr MORAS Dino, Dr POTERSZMAN Arnaud, Dr VAN DORSSELAER Alain
Tous les auteurs :
Fribourg S, Kellenberger E, Rogniaux H, Poterszman A, Van Dorsselaer A, Thierry JC, Egly JM, Moras D, Kieffer B
Lien Pubmed
Résumé
In an effort to understand the structure function relationship of TFIIH, a transcription/repair factor, we focused our attention on the p44 subunit, which plays a central role in both mechanisms. The amino-terminal portion of p44 has been shown to be involved in the regulation of the XPD helicase activity; here we show that its carboxyl-terminal domain is essential for TFIIH transcription activity and that it binds three zinc atoms through two independent modules. The first contains a C4 zinc finger motif, whereas the second is characterized by a CX(2)CX(2-4)FCADCD motif, corresponding to interleaved zinc binding sites. The solution structure of this second module reveals an unexpected homology with the regulatory domain of protein kinase C and provides a framework to study its role at the molecular level.
Référence
J Biol Chem. 2000 Oct 13;275(41):31963-71.