期刊
MOLECULAR CELL
卷 23, 期 6, 页码 801-808出版社
CELL PRESS
DOI: 10.1016/j.molcel.2006.07.019
关键词
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资金
- Biotechnology and Biological Sciences Research Council [BB/C007077/1] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/C007077/1] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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.
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