Inhibition of RecA-mediated cleavage in covalent dimers of UmuD.
Disulfide-cross-linked UmuD2 derivatives were cleaved poorly upon incubation with activated RecA. Reducing the disulfide bonds prior to incubating the derivatives with RecA dramatically increased their extent of cleavage. These observations suggest that the UmuD monomer is a better substrate for the RecA-mediated cleavage reaction than the dimer.
Lee
M H
MH
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
Guzzo
A
A
Walker
G C
GC
D001426:Bacterial Proteins / Q000378:metabolism*; D003545:Cysteine; D004259:DNA-Directed DNA Polymerase; D004220:Disulfides; D004229:Dithiothreitol; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D011938:Rec A Recombinases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004220:Disulfides; D029968:Escherichia coli Proteins; D011938:Rec A Recombinases; D004259:DNA-Directed DNA Polymerase; C055218:UmuD protein, E coli; D003545:Cysteine; D004229:Dithiothreitol