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FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein.

Blood | Oct 1, 2007

http://www.ncbi.nlm.nih.gov/pubmed/17596542

The BRCA1 associated C-terminal helicase (BACH1, designated FANCJ) is implicated in the chromosomal instability genetic disorder Fanconi anemia (FA) and hereditary breast cancer. A critical role of FANCJ helicase may be to restart replication as a component of downstream events that occur during the repair of DNA cross-links or double-strand breaks. We investigated the potential interaction of FANCJ with replication protein A (RPA), a single-stranded DNA-binding protein implicated in both DNA replication and repair. FANCJ and RPA were shown to coimmunoprecipitate most likely through a direct interaction of FANCJ and the RPA70 subunit. Moreover, dependent on the presence of BRCA1, FANCJ colocalizes with RPA in nuclear foci after DNA damage. Our data are consistent with a model in which FANCJ associates with RPA in a DNA damage-inducible manner and through the protein interaction RPA stimulates FANCJ helicase to better unwind duplex DNA substrates. These findings identify RPA as the first regulatory partner of FANCJ. The FANCJ-RPA interaction is likely to be important for the role of the helicase to more efficiently unwind DNA repair intermediates to maintain genomic stability.

Pubmed ID: 17596542 RIS Download

Mesh terms: Basic-Leucine Zipper Transcription Factors | Cell Line | DNA Damage | DNA Helicases | DNA-Binding Proteins | Fanconi Anemia | Fanconi Anemia Complementation Group Proteins | Humans | Kinetics | Mutation | Protein Binding | RNA, Small Interfering | Replication Protein A

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Associated grants

  • Agency: Intramural NIH HHS, Id:

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