RecA dimers serve as a functional unit for assembly of active nucleoprotein filaments.
All RecA-like recombinase enzymes catalyze DNA strand exchange as elongated filaments on DNA. Despite numerous biochemical and structural studies of RecA and the related Rad51 and RadA proteins, the unit oligomer(s) responsible for nucleoprotein filament assembly and coordinated filament activity remains undefined. We have created a RecA fused dimer protein and show that it maintains in vivo DNA repair and LexA co-protease activities, as well as in vitro ATPase and DNA strand exchange activities. Our results support the idea that dimeric RecA is an important functional unit both for assembly of nucleoprotein filaments and for their coordinated activity during the catalysis of homologous recombination.
Forget
Anthony L
AL
Department of Biochemistry and Molecular Pharmacology, Aaron Lazare Research Building, 364 Plantation Street, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
Kudron
Michelle M
MM
McGrew
Dharia A
DA
Calmann
Melissa A
MA
Schiffer
Celia A
CA
Knight
Kendall L
KL
D000251:Adenosine Triphosphatases / Q000378:metabolism; D019281:Dimerization; D009698:Nucleoproteins / Q000378:metabolism* / Q000648:ultrastructure; D011938:Rec A Recombinases / Q000235:genetics / Q000502:physiology*; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D009698:Nucleoproteins; D011993:Recombinant Fusion Proteins; D011938:Rec A Recombinases; D000251:Adenosine Triphosphatases