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 m
any of these mutant proteins exist in a more homogeneous oligomeric fo
rm, which approximates to the size of a RecA hexamer. Some of these mu
tants have a significant level of activity in vivo for recombinational
DNA repair and thus represent the first mutant RecA proteins identifi
ed which retain activity yet can exist in a discrete oligomeric state
as free protein. (C) 1997 Academic Press Limited.