Abstract
In Escherichia coli, phosphoryl substituents in the lipopolysaccharide core region are essential for outer membrane stability. Mutation of the core glucosyltransferase encoded by waaG (formerly rfaG) resulted in lipopolysaccharide truncated immediately after the inner core heptose residues, which serve as the sites for phosphorylation. Surprisingly, mutation of waaG also destabilized the outer membrane. Structural analyses of waaG mutant lipopolysaccharide showed that the cause for this phenotype was a decrease in core phosphorylation, an unexpected side effect of the waaG mutation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acylation
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Bacterial Outer Membrane Proteins / analysis
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Carbohydrate Sequence
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / drug effects
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins*
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Glucosyltransferases / genetics
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Glucosyltransferases / metabolism*
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Hydrolysis
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Lipopolysaccharides / isolation & purification
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Lipopolysaccharides / metabolism*
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Molecular Sequence Data
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Mutagenesis
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Novobiocin / metabolism
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Oligosaccharides / metabolism
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Phenotype
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Phosphorylation
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Sodium Dodecyl Sulfate / pharmacology
Substances
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Bacterial Outer Membrane Proteins
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Bacterial Proteins
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Escherichia coli Proteins
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Lipopolysaccharides
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Oligosaccharides
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Novobiocin
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Sodium Dodecyl Sulfate
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Glucosyltransferases
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WaaG protein, E coli