Inhibition of Escherichia coli RecA by rationally redesigned N-terminal helix.
Bacterial RecA promotes the development and transmission of antibiotic resistance genes by self-assembling into an ATP-hydrolyzing filamentous homopolymer on single-stranded DNA. We report the design of a 29mer peptide based on the RecA N-terminal domain involved in intermonomer contact that inhibits RecA filament assembly with an IC50 of 3 microM.
Cline
Daniel J
DJ
School of Pharmacy, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7360, USA.
Holt
Shannon L
SL
Singleton
Scott F
SF
D000251:Adenosine Triphosphatases / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry; D000595:Amino Acid Sequence; D002626:Chemistry, Pharmaceutical / Q000379:methods; D004277:DNA, Single-Stranded / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology*; D020128:Inhibitory Concentration 50; D008954:Models, Biological; D008969:Molecular Sequence Data; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011938:Rec A Recombinases / Q000037:antagonists & inhibitors*
D004277:DNA, Single-Stranded; D004791:Enzyme Inhibitors; D011108:Polymers; D000255:Adenosine Triphosphate; D011938:Rec A Recombinases; D000251:Adenosine Triphosphatases