Understanding the Role of Replication Protein A and RAD52 in Breast Cancer

2004 ◽  
Author(s):  
Gloria E. Borgstahl
Keyword(s):  
Breast Cancer ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein

scholarly journals 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 ◽  
2007 ◽  
Vol 110 (7) ◽  
pp. 2390-2398 ◽  
Author(s):  
Rigu Gupta ◽  
Sudha Sharma ◽  
Joshua A. Sommers ◽  
Mark K. Kenny ◽  
Sharon B. Cantor ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Binding ◽  
Binding Protein ◽  
Critical Role ◽  
Protein A ◽  
Replication Protein A ◽  
Dna Binding Protein ◽  
Replication Protein ◽  
Single Stranded Dna

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.

scholarly journals Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing

Open Biology ◽  
2011 ◽  
Vol 1 (4) ◽  
pp. 110023 ◽  
Author(s):  
Yuko Akai ◽  
Yumiko Kurokawa ◽  
Norihiko Nakazawa ◽  
Yuko Tonami-Murakami ◽  
Yuki Suzuki ◽  
...  
Keyword(s):  
Protein A ◽  
Coiled Coil ◽  
Replication Protein A ◽  
Replication Protein ◽  
Mutation Site ◽  
Damage Repair ◽  
Dna Strands ◽  
Structural Maintenance Of Chromosomes

Condensin is required for chromosome dynamics and diverse DNA metabolism. How condensin works, however, is not well understood. Condensin contains two structural maintenance of chromosomes (SMC) subunits with the terminal globular domains connected to coiled-coil that is interrupted by the central hinge. Heterotrimeric non-SMC subunits regulate SMC. We identified a novel fission yeast SMC hinge mutant, cut14-Y1 , which displayed defects in DNA damage repair and chromosome segregation. It contains an amino acid substitution at a conserved hinge residue of Cut14/SMC2, resulting in diminished DNA binding and annealing. A replication protein A mutant, ssb1-418 , greatly alleviated the repair and mitotic defects of cut14-Y1 . Ssb1 protein formed nucleolar foci in cut14-Y1 cells, but the number of foci was diminished in cut14-Y1 ssb1-418 double mutants. Consistent with the above results, Ssb1 protein bound to single-strand DNA was removed by condensin or the SMC dimer through DNA reannealing in vitro . Similarly, RNA hybridized to DNA may be removed by the SMC dimer. Thus, condensin may wind up DNA strands to unload chromosomal components after DNA repair and prior to mitosis. We show that 16 suppressor mutations of cut14-Y1 were all mapped within the hinge domain, which surrounded the original L543 mutation site.

The role of p14 subunit of replication protein A in binding to single-stranded DNA

2007 ◽  
Vol 412 (1) ◽  
pp. 4-7 ◽  
Author(s):  
P. E. Pestryakov ◽  
Yu. S. Krasikova ◽  
I. O. Petruseva ◽  
S. N. Khodyreva ◽  
O. I. Lavrik
Keyword(s):  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Single Stranded Dna

scholarly journals In VitroAnalysis of the Role of Replication Protein A (RPA) and RPA Phosphorylation in ATR-mediated Checkpoint Signaling

2012 ◽  
Vol 287 (43) ◽  
pp. 36123-36131 ◽  
Author(s):  
Laura A. Lindsey-Boltz ◽  
Joyce T. Reardon ◽  
Marc S. Wold ◽  
Aziz Sancar
Keyword(s):  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Checkpoint Signaling
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