The Fanconi anemia protein FANCM can promote branch migration of Holliday junctions and replication forks.

Détails

ID Serval
serval:BIB_5826A5E32C17
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The Fanconi anemia protein FANCM can promote branch migration of Holliday junctions and replication forks.
Périodique
Molecular Cell
Auteur(s)
Gari K., Décaillet C., Stasiak A.Z., Stasiak A., Constantinou A.
ISSN
1097-2765 (Print)
ISSN-L
1097-2765
Statut éditorial
Publié
Date de publication
01/2008
Peer-reviewed
Oui
Volume
29
Numéro
1
Pages
141-148
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Fanconi anemia (FA) is a genetically heterogeneous cancer-prone disorder associated with chromosomal instability and cellular hypersensitivity to DNA crosslinking agents. The FA pathway is suspected to play a crucial role in the cellular response to DNA replication stress. At a molecular level, however, the function of most of the FA proteins is unknown. FANCM displays DNA-dependent ATPase activity and promotes the dissociation of DNA triplexes, but the physiological significance of this activity remains elusive. Here we show that purified FANCM binds to Holliday junctions and replication forks with high specificity and promotes migration of their junction point in an ATPase-dependent manner. Furthermore, we provide evidence that FANCM can dissociate large recombination intermediates, via branch migration of Holliday junctions through 2.6 kb of DNA. Our data suggest a direct role for FANCM in DNA processing, consistent with the current view that FA proteins coordinate DNA repair at stalled replication forks.
Mots-clé
Adenosine Triphosphate/metabolism, Adenylyl Imidodiphosphate/metabolism, Animals, Cell Line/chemistry, Chromatography, Affinity, DNA Helicases/genetics, DNA Helicases/isolation & purification, DNA Replication/physiology, DNA, Cruciform/metabolism, DNA-Binding Proteins/physiology, Dimerization, Electrophoretic Mobility Shift Assay, Humans, Microscopy, Electron, Oligodeoxyribonucleotides/chemical synthesis, Oligodeoxyribonucleotides/metabolism, Protein Binding, Recombinant Fusion Proteins/isolation & purification, Recombinant Fusion Proteins/physiology, Recombination, Genetic/physiology, Spodoptera, Substrate Specificity
Pubmed
Web of science
Open Access
Oui
Création de la notice
31/01/2008 15:30
Dernière modification de la notice
20/08/2019 15:11
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