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

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

doi:10.1016/j.molcel.2006.07.019

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

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

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

292 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)	801-808
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

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

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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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author = "J Rudolf and V Makrantoni and Ingledew, {William John} and Stark, {M J R} and White, {Malcolm Frederick}",

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

AU - Rudolf, J

AU - Makrantoni, V

AU - Ingledew, William John

AU - Stark, M J R

AU - White, Malcolm Frederick

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 - ENZYME ENDONUCLEASE-III

KW - SACCHAROMYCES-CEREVISIAE

KW - ESCHERICHIA-COLI

KW - XERODERMA-PIGMENTOSUM

KW - FACTOR TFIIH

KW - PROTEIN

KW - GENE

KW - TRANSCRIPTION

KW - TRICHOTHIODYSTROPHY

KW - BACH1

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U2 - 10.1016/j.molcel.2006.07.019

DO - 10.1016/j.molcel.2006.07.019

M3 - Article

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

Keywords

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