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.
Logan
K M
KM
Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, Worcester 01655, USA.
Skiba
M C
MC
Eldin
S
S
Knight
K L
KL
D001120:Arginine / Q000235:genetics; D001216:Asparagine / Q000235:genetics; D001419:Bacteria / Q000737:chemistry; D002853:Chromatography, Liquid / Q000379:methods; D018360:Crystallography, X-Ray; D004260:DNA Repair; D008239:Lysine / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D010649:Phenylalanine / Q000235:genetics; D011487:Protein Conformation; D011938:Rec A Recombinases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D014443:Tyrosine / Q000235:genetics
D014443:Tyrosine; D010649:Phenylalanine; D001216:Asparagine; D001120:Arginine; D011938:Rec A Recombinases; D008239:Lysine