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

Research output: Contribution to journalArticle

Author(s)

J Rudolf, V Makrantoni, William John Ingledew, M J R Stark, Malcolm Frederick White

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Abstract

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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Original languageEnglish
Pages (from-to)801-808
Number of pages8
JournalMolecular Cell
Volume23
Issue number6
DOIs
Publication statusPublished - 15 Sep 2006

    Research areas

  • ENZYME ENDONUCLEASE-III, SACCHAROMYCES-CEREVISIAE, ESCHERICHIA-COLI, XERODERMA-PIGMENTOSUM, FACTOR TFIIH, PROTEIN, GENE, TRANSCRIPTION, TRICHOTHIODYSTROPHY, BACH1

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