Abstract
The RecX protein is a potent inhibitor of RecA activities. We identified several factors that affect RecX-RecA interaction. The interaction is enhanced by the RecA C terminus and by significant concentrations of free Mg(2+) ion. The interaction is also enhanced by an N-terminal His(6) tag on the RecX protein. We conclude that RecX protein interacts most effectively with a RecA functional state designated A(o) and that the RecA C terminus has a role in modulating the interaction. We further identified a C-terminal point mutation in RecA protein (E343K) that significantly alters the interaction between RecA and RecX proteins.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphate / chemistry
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Bacterial Proteins / chemistry
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Bacterial Proteins / physiology*
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Buffers
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Cloning, Molecular
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DNA / chemistry
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DNA, Single-Stranded / chemistry
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / metabolism
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Escherichia coli / physiology*
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Escherichia coli Proteins / physiology
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Gene Expression Regulation, Bacterial
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Hydrolysis
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Ions
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Magnesium / chemistry
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Point Mutation
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Protein Structure, Tertiary
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Rec A Recombinases / antagonists & inhibitors*
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Rec A Recombinases / chemistry
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Time Factors
Substances
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Bacterial Proteins
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Buffers
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DNA, Single-Stranded
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Escherichia coli Proteins
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Ions
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RecX protein, Xanthomonas campestris
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Adenosine Triphosphate
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DNA
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Rec A Recombinases
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Adenosine Triphosphatases
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Magnesium