TY - JOUR
T1 - Role of replication protein a in double holliday junction dissolution mediated by the BLM-Topo IIIα-RMI1-RMI2 protein complex
AU - Xue, Xiaoyu
AU - Raynard, Steven
AU - Busygina, Valeria
AU - Singh, Akhilesh K.
AU - Sung, Patrick
PY - 2013/5/17
Y1 - 2013/5/17
N2 - The conserved BTR complex, composed of the Bloom's syndrome helicase (BLM), topoisomerase IIIα, 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.
AB - The conserved BTR complex, composed of the Bloom's syndrome helicase (BLM), topoisomerase IIIα, 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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U2 - 10.1074/jbc.M113.465609
DO - 10.1074/jbc.M113.465609
M3 - Article
C2 - 23543748
AN - SCOPUS:84877898746
SN - 0021-9258
VL - 288
SP - 14221
EP - 14227
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 20
ER -