Abstract
We report that N(6)-(1-naphthyl)-ADP inhibits the Escherichia coli RecA protein in vitro. A novel rapid screen identified it as a potent inhibitor of RecA nucleoprotein filament formation, and further characterization established it as an ATP-competitive inhibitor of RecA-catalyzed ATP hydrolysis. This and other inhibitors of RecA activities represent a new approach for understanding the molecular targets and pathways involved in the evolution of antibiotic resistance in bacteria.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
1-Naphthylamine / analogs & derivatives*
-
1-Naphthylamine / chemical synthesis
-
1-Naphthylamine / chemistry
-
Adenosine Diphosphate / analogs & derivatives*
-
Adenosine Diphosphate / chemical synthesis
-
Adenosine Diphosphate / chemistry
-
Adenosine Triphosphate / chemistry
-
DNA, Single-Stranded / chemistry
-
Drug Resistance, Bacterial*
-
Escherichia coli Proteins / chemistry*
-
Hydrolysis
-
Kinetics
-
Models, Molecular
-
Protein Binding
-
Rec A Recombinases / antagonists & inhibitors*
-
Rec A Recombinases / chemistry*
-
Structure-Activity Relationship
Substances
-
DNA, Single-Stranded
-
Escherichia coli Proteins
-
N(6)-(1-naphthyl)adenosine diphosphate
-
Adenosine Diphosphate
-
Adenosine Triphosphate
-
1-Naphthylamine
-
Rec A Recombinases