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

Jana Rudolf; Vasso Makrantoni; W. John Ingledew; Michael J. R. Stark; Malcolm F. White

doi:10.1016/j.molcel.2006.07.019

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

Jana Rudolf, Vasso Makrantoni, W. John Ingledew, Michael J. R. Stark, Malcolm F. White

Research output: Contribution to journal › Article › peer-review

295 Citations (Scopus)

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.

Original language	English
Pages (from-to)	801-8
Number of pages	8
Journal	Molecular Cell
Volume	23
Issue number	6
DOIs	https://doi.org/10.1016/j.molcel.2006.07.019
Publication status	Published - 15 Sept 2006

Keywords

DNA

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10.1016/j.molcel.2006.07.019

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title = "The DNA repair helicases XPD and FancJ have essential iron-sulfur domains",

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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T1 - The DNA repair helicases XPD and FancJ have essential iron-sulfur domains

AU - Rudolf, Jana

AU - Makrantoni, Vasso

AU - Ingledew, W. John

AU - Stark, Michael J. R.

AU - White, Malcolm F.

PY - 2006/9/15

Y1 - 2006/9/15

N2 - 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.

AB - 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.

KW - DNA

U2 - 10.1016/j.molcel.2006.07.019

DO - 10.1016/j.molcel.2006.07.019

M3 - Article

C2 - 16973432

SN - 1097-2765

VL - 23

SP - 801

EP - 808

JO - Molecular Cell

JF - Molecular Cell

IS - 6

ER -

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

Abstract

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