Abstract
The human recombinase hRad51 is a key protein for the maintenance of genome integrity and for cancer development. This protein plays a central role is the DNA strand exchange occurring during homologous recombination. Here we report the polymerization and depolymerization of hRad51 on duplex DNA observed with a new generation of magnetic tweezers, allowing the measurement of DNA twist with a resolution of 5° in real time. At odds with earlier claims, we show that, after initial deposition of a multimeric nucleus, nucleoprotein filament growth occurs by addition of single proteins, involving DNA twisting steps of 65±5°.
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