Abstract
The RecA nucleoprotein filament formed on double-stranded (ds) DNA exhibits a functional state comparable to the state observed during active DNA strand exchange. By stretching short DNA of only a few hundreds base pairs, we observed high-resolution saw-tooth dynamics of RecA polymerization and de-polymerization on a single dsDNA molecule that was unable to be seen in previous single-DNA stretching experiments when much longer DNA was used. Novel saw-tooth fluctuation of the nucleoprotein filament was observed, allowing us to monitor the real time competition between RecA on and off DNA strands driven by the ATP-hydrolysis at a nanometer resolution.
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