17596542

Source:http://linkedlifedata.com/resource/pubmed/id/17596542

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0012860, umls-concept:C0037183, umls-concept:C0165675, umls-concept:C0205234, umls-concept:C0205263, umls-concept:C0376315, umls-concept:C0920283, umls-concept:C1412729, umls-concept:C1426958
pubmed:issue	7
pubmed:dateCreated	2007-9-20
pubmed:abstractText	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.
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7603509
pubmed:citationSubset	AIM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/BACH1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Basic-Leucine Zipper Transcription..., http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fanconi Anemia Complementation..., http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering, http://linkedlifedata.com/resource/pubmed/chemical/Replication Protein A
pubmed:status	MEDLINE
pubmed:month	Oct
pubmed:issn	0006-4971
pubmed:author	pubmed-author:BroshRobert MRMJr, pubmed-author:CantorSharon BSB, pubmed-author:GuptaRiguR, pubmed-author:KennyMark KMK, pubmed-author:SharmaSudhaS, pubmed-author:SommersJoshua AJA
pubmed:issnType	Print
pubmed:day	1
pubmed:volume	110
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	2390-8
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:17596542-Basic-Leucine Zipper Transcription Factors, pubmed-meshheading:17596542-Cell Line, pubmed-meshheading:17596542-DNA Damage, pubmed-meshheading:17596542-DNA Helicases, pubmed-meshheading:17596542-DNA-Binding Proteins, pubmed-meshheading:17596542-Fanconi Anemia, pubmed-meshheading:17596542-Fanconi Anemia Complementation Group Proteins, pubmed-meshheading:17596542-Humans, pubmed-meshheading:17596542-Kinetics, pubmed-meshheading:17596542-Mutation, pubmed-meshheading:17596542-Protein Binding, pubmed-meshheading:17596542-RNA, Small Interfering, pubmed-meshheading:17596542-Replication Protein A
pubmed:year	2007
pubmed:articleTitle	FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein.
pubmed:affiliation	Laboratory of Molecular Gerontology, National Institute on Aging (NIA), National Institutes of Health (NIH), Baltimore, MD 21224, USA.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't

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