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- W1562361795 endingPage "e1002213" @default.
- W1562361795 startingPage "e1002213" @default.
- W1562361795 abstract "Repair of DNA breaks by single-strand annealing (SSA) is a major mechanism for the maintenance of genomic integrity. SSA is promoted by proteins (single-strand-annealing proteins [SSAPs]), such as eukaryotic RAD52 and λ phage Redβ. These proteins use a short single-stranded region to find sequence identity and initiate homologous recombination. However, it is unclear how SSAPs detect homology and catalyze annealing. Using single-molecule experiments, we provide evidence that homology is recognized by Redβ monomers that weakly hold single DNA strands together. Once annealing begins, dimerization of Redβ clamps the double-stranded region and nucleates nucleoprotein filament growth. In this manner, DNA clamping ensures and secures a successful detection for DNA sequence homology. The clamp is characterized by a structural change of Redβ and a remarkable stability against force up to 200 pN. Our findings not only present a detailed explanation for SSAP action but also identify the DNA clamp as a very stable, noncovalent, DNA-protein interaction." @default.
- W1562361795 created "2016-06-24" @default.
- W1562361795 creator A5044530391 @default.
- W1562361795 creator A5051546849 @default.
- W1562361795 creator A5053220755 @default.
- W1562361795 creator A5067642016 @default.
- W1562361795 creator A5086267534 @default.
- W1562361795 date "2015-08-13" @default.
- W1562361795 modified "2023-10-16" @default.
- W1562361795 title "A Single-Strand Annealing Protein Clamps DNA to Detect and Secure Homology" @default.
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