Structural characterization of the cysteine-rich domain of TFIIH p44 subunit

被引:26
作者
Fribourg, S
Kellenberger, E
Rogniaux, H
Poterszman, A
Van Dorsselaer, A
Thierry, JC
Egly, JM
Moras, D
Kieffer, B
机构
[1] ULP, INSERM, CNRS, Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch, France
[2] Ecole Super Biotechnol Strasbourg, CNRS UPR 9004, Communaunte Urbaine Strasbourg, F-67400 Illkirch Graffenstaden, France
[3] Ecole Super Biotechnol Strasbourg, CNRS UPR 9004, Lab Resonance Magnet, F-67400 Illkirch Graffenstaden, France
[4] ULP, CNRS UMR 7509, Lab Spectrometrie Masse Bio Organ, F-67008 Strasbourg, France
关键词
D O I
10.1074/jbc.M004960200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:31963 / 31971
页数:9
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