Abstract
The Escherichia coli gene hflX was first identified as part of the hflA operon, mutations in which led to an increased frequency of lysogenization upon infection of the bacterium by the temperate coliphage lambda. Independent mutational studies have also indicated that the HflX protein has a role in transposition. Based on the sequence of its gene, HflX is predicted to be a GTP-binding protein, very likely a GTPase. We report here purification and characterization of the HflX protein. We also specifically examined its suggested functional roles mentioned above. Our results show that HflX is a monomeric protein with a high (30% to 40%) content of helices. It exhibits GTPase as well as ATPase activities, but it has no role in lambda lysogeny or in transposition.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / isolation & purification
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Adenosine Triphosphatases / metabolism*
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Bacteriophage lambda / physiology
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Escherichia coli / chemistry
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli / virology
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / isolation & purification
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Escherichia coli Proteins / metabolism*
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GTP Phosphohydrolases / chemistry
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GTP Phosphohydrolases / genetics
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GTP Phosphohydrolases / isolation & purification
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GTP Phosphohydrolases / metabolism*
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GTP-Binding Proteins / chemistry
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GTP-Binding Proteins / genetics
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GTP-Binding Proteins / isolation & purification
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GTP-Binding Proteins / metabolism*
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Lysogeny
Substances
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Escherichia coli Proteins
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Adenosine Triphosphatases
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GTP Phosphohydrolases
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GTP-Binding Proteins
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HflX protein, E coli