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Publication : Role of replication protein A in double holliday junction dissolution mediated by the BLM-Topo IIIα-RMI1-RMI2 protein complex.

First Author  Xue X Year  2013
Journal  J Biol Chem Volume  288
Issue  20 Pages  14221-14227
PubMed ID  23543748 Mgi Jnum  J:319969
Mgi Id  MGI:6867134 Doi  10.1074/jbc.M113.465609
Citation  Xue X, et al. (2013) Role of replication protein A in double holliday junction dissolution mediated by the BLM-Topo IIIalpha-RMI1-RMI2 protein complex. J Biol Chem 288(20):14221-14227
abstractText  The conserved BTR complex, composed of the Bloom's syndrome helicase (BLM), topoisomerase IIIalpha, RMI1, and RMI2, regulates homologous recombination in favor of non-crossover formation via the dissolution of the double Holliday Junction (dHJ). Here we show enhancement of the BTR-mediated dHJ dissolution reaction by the heterotrimeric single-stranded DNA binding protein replication protein A (RPA). Our results suggest that RPA acts by sequestering a single-stranded DNA intermediate during dHJ dissolution. We provide evidence that RPA physically interacts with RMI1. The RPA interaction domain in RMI1 has been mapped, and RMI1 mutants impaired for RPA interaction have been generated. Examination of these mutants ascertains the significance of the RMI1-RPA interaction in dHJ dissolution. Our results thus implicate RPA as a cofactor of the BTR complex in dHJ dissolution.
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