Description
RecA, which functions in DNA recombination and DNA repair, binds to single stranded DNA, resulting in the polymerization of RecA into a nucleoprotein complex. This complex aligns with complementary-double stranded DNA, resulting in RecA catalysis of DNA strand exchange. RecA DNA binding is stimulated by ATP hydrolysis or non-hydrolyzable ATP analogs. The RecA–ATP–single-stranded DNA complex also functions as a coprotease factor in the proteolytic cleavage of LexA, UmuD and certain bacteriophage proteins. RecA complexed with site-specific oligonucleotides has been used to target and specifically cleave large DNA fragments