Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphate / chemistry
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Amino Acid Sequence
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Chemistry, Pharmaceutical / methods
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DNA, Single-Stranded / metabolism
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Enzyme Inhibitors / chemical synthesis*
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Enzyme Inhibitors / chemistry
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Escherichia coli / enzymology*
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Inhibitory Concentration 50
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Models, Biological
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Molecular Sequence Data
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Polymers / chemistry
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Rec A Recombinases / antagonists & inhibitors*
Substances
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DNA, Single-Stranded
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Enzyme Inhibitors
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Polymers
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Adenosine Triphosphate
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Rec A Recombinases
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Adenosine Triphosphatases