Mutant RecA proteins which form hexamer-sized oligomers.

We have analyzed the oligomeric properties of a number of mutant RecA proteins containing single amino acid substitutions within one region of the subunit interface. In contrast to wild-type RecA, which forms a heterogeneous population of different-sized oligomers, we find that many of these mutant proteins exist in a more homogeneous oligomeric form, which approximates to the size of a RecA hexamer. Some of these mutants have a significant level of activity in vivo for recombinational DNA repair and thus represent the first mutant RecA proteins identified which retain activity yet can exist in a discrete oligomeric state as free protein.