原创力文档role of saccharomyces single-stranded dna-binding protein rpa in the strand invasion step of double-strand break repair酿酒的单链dna结合蛋白质链入侵步战的双链断裂修复.pdfVIP
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role of saccharomyces single-stranded dna-binding protein rpa in the strand invasion step of double-strand break repair酿酒的单链dna结合蛋白质链入侵步战的双链断裂修复
PLoS BIOLOGY
Role of Saccharomyces Single-Stranded
DNA-Binding Protein RPA in the Strand
Invasion Step of Double-Strand Break Repair
*
Xuan Wang, James E. Haber
Rosenstiel Center and Department of Biology, Brandeis University, Waltham, Massachusetts, United States of America
The single-stranded DNA (ssDNA)-binding protein replication protein A (RPA) is essential for both DNA replication and
recombination. Chromatin immunoprecipitation techniques were used to visualize the kinetics and extent of RPA
binding following induction of a double-strand break (DSB) and during its repair by homologous recombination in
yeast. RPA assembles at the HO endonuclease-cut MAT locus simultaneously with the appearance of the DSB, and
binding spreads away from the DSB as 59 to 39 exonuclease activity creates more ssDNA. RPA binding precedes binding
of the Rad51 recombination protein. The extent of RPA binding is greater when Rad51 is absent, supporting the idea
that Rad51 displaces RPA from ssDNA. RPA plays an important role during RAD51-mediated strand invasion of the MAT
ssDNA into the donor sequence HML. The replication-proficient but recombination-defective rfa1-t11 (K45E) mutation
in the large subunit of RPA is normal in facilitating Rad51 filament formation on ssDNA, but is unable to achieve
synapsis between MAT and HML. Thus, RPA appears to play a role in strand invasion as well as in facilitating Rad51
binding to ssDNA, possibly by stabilizing the displaced ssDNA.
Introduction homologue RecA to polymerize across regions that contain
secondary structures (Shibata et al. 1980; West e
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