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Blood, 1 October 2007, Vol. 110, No. 7, pp. 2390-2398.
Prepublished online as a Blood First Edition Paper on June 27, 2007; DOI 10.1182/blood-2006-11-057273.
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Submitted November 14, 2006
Accepted June 22, 2007
FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA binding protein
Rigu Gupta, Sudha Sharma, Joshua A. Sommers, Mark K. Kenny, Sharon B. Cantor, and Robert M. Brosh Jr.*
Laboratory of Molecular Gerontology, National Institute on Aging, NIH, Baltimore, MD, United States
Department of Emergency Medicine, Albert Einstein College of Medicine, Montefiore Medical Center, Bronx, NY, United States
Department of Cancer Biology, University of Massachusetts Medical School, Lazare Research Building, Worcester, MA, United States
* Corresponding author; email: broshr{at}grc.nia.nih.gov.
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 co-immunoprecipitate most likely through a direct interaction of FANCJ and the RPA70 subunit. Moreover, dependent on the presence of BRCA1, FANCJ co-localizes 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.
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