The DNA repair helicases XPD and FancJ have essential iron-sulfur domains.
Mol Cell
; 23(6): 801-8, 2006 Sep 15.
Article
en En
| MEDLINE
| ID: mdl-16973432
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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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Arqueales
/
Enzimas Reparadoras del ADN
/
Proteína de la Xerodermia Pigmentosa del Grupo D
/
Proteínas del Grupo de Complementación de la Anemia de Fanconi
/
Proteínas Hierro-Azufre
Idioma:
En
Revista:
Mol Cell
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2006
Tipo del documento:
Article
País de afiliación:
Reino Unido
Pais de publicación:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
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US
/
USA