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• W2775471907 abstract "Genomic integrity, when compromised by accrued DNA lesions, is maintained through efficient repair via homologous recombination. For this process the ubiquitous recombinase A (RecA), and its homologues such as the human Rad51, are of central importance, able to align and exchange homologous sequences within single-stranded and double-stranded DNA in order to swap out defective regions. Here, we directly observe the widely debated mechanism of RecA homology searching at a single-molecule level using high-speed atomic force microscopy (HS-AFM) in combination with tailored DNA origami frames to present the reaction targets in a way suitable for AFM-imaging. We show that RecA nucleoprotein filaments move along DNA substrates via short-distance facilitated diffusions, or slides, interspersed with longer-distance random moves, or hops. Importantly, from the specific interaction geometry, we find that the double-stranded substrate DNA resides in the secondary DNA binding-site within the RecA nucleoprotein filament helical groove during the homology search. This work demonstrates that tailored DNA origami, in conjunction with HS-AFM, can be employed to reveal directly conformational and geometrical information on dynamic protein-DNA interactions which was previously inaccessible at an individual single-molecule level." @default.
• W2775471907 created "2017-12-22" @default.
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• W2775471907 date "2017-12-12" @default.
• W2775471907 modified "2023-10-14" @default.
• W2775471907 title "Direct Single-Molecule Observation of Mode and Geometry of RecA-Mediated Homology Search" @default.
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• W2775471907 doi "https://doi.org/10.1021/acsnano.7b06208" @default.
• W2775471907 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29202219" @default.
• W2775471907 hasPublicationYear "2017" @default.
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