Abstract
In Escherichia coli, the RecA nucleoprotein filament formed on single-stranded DNA (ssDNA) is essential for homologous recombinational DNA damage repair. In vivo, formation and stability of the RecA nucleoprotein filament is regulated by the single-stranded DNA binding protein (SSB). However, current understanding of RecA-ssDNA interaction has been mainly based on experiments in the absence of SSB. In this study, direct knowledge of the influence of SSB on the RecA nucleation, polymerization, and stability is obtained by single ssDNA manipulation method using magnetic tweezers. Our results reveal an SSB, force, and ATP hydrolysis dependent regulation of the RecA nucleoprotein filament formation and stability.
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