Elongation of duplex DNA by recA protein

Abstract recA protein, which is essential for the recombination process in Escherichia coli , was incubated in the presence of 5′-γ-thiotriphosphate with circular plasmid pBR β G containing small single-stranded gaps. Stable complexes were formed which appear in the electron microscope as fibres with a diameter about five times that of naked DNA. Complex formation appears to be a co-operative process whereby the average rise per base-pair with respect to the fibre axis increases from 3·39 ± 0·08 A to 5·20 ± 0·18 A. The elongation of DNA by about 50% is compatible with an unwinding of the double helix and an intercalating mode of binding of recA and/or 5′-γ-thiotriphosphate to DNA.