The DNA repair helicases XPD and FancJ have essential iron-sulfur domains

被引：274

作者：

Rudolf, Jana

Makrantoni, Vasso

Ingledew, W. John

Stark, Michael J. R.

White, Malcolm F.

机构：

[1] Univ St Andrews, Ctr Biomol Sci, St Andrews KY16 9ST, Fife, Scotland

[2] Univ Dundee, Sch Life Sci, Div Gene Regulat & Express, Dundee DD1 5EH, Scotland

来源：

MOLECULAR CELL | 2006年 / 23卷 / 06期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/j.molcel.2006.07.019

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：

DNA helicases are essential components of the cellular machinery for DNA replication, recombination, repair, and transcription. The XPD and FancJ proteins are related helicases involved in the nucleotide excision repair (NER) and Fanconi anemia repair pathways, respectively. We demonstrate that both proteins have a conserved domain near the N terminus that includes an iron-sulfur (Fe-S) cluster. Three absolutely conserved cysteine residues provide ligands for the Fe-S cluster, which is essential for the helicase activity of XPD. Yeast strains harboring mutations in the Fe-S domain of Rad3 (yeast XPD) are defective in excision repair of UV photoproducts. Clinically relevant mutations in patients with trichothiodystrophy (TTD) and Fanconi anemia disrupt the Fe-S clusters of XPD and FancJ and thereby abolish helicase activity.

引用

收藏

页码：801 / 808

页数：8

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