Abstract
The LptA protein of Escherichia coli has been implicated in the transport of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Here we provide evidence that LptA binds structurally diverse LPS substrates in vitro and demonstrate that it interacts specifically with the lipid A domain of LPS. These results are consistent with LptA playing a chaperone role in the transport of LPS across the periplasm and have implications for possible assembly models.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Acyltransferases / genetics
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Acyltransferases / isolation & purification
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Acyltransferases / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Lipid A / chemistry
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Lipid A / metabolism*
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Lipopolysaccharides / metabolism*
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Molecular Structure
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Phosphatidylethanolamines / metabolism
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Protein Binding
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Solubility
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Substrate Specificity
Substances
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Lipid A
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Lipopolysaccharides
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Phosphatidylethanolamines
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phosphatidylethanolamine
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Acyltransferases
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acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferase