Abstract
The formation of the Staphylococcus aureus peptidoglycan pentaglycine interpeptide chain needs FemA and FemB for the incorporation of glycines Gly2-Gly3, and Gly4-Gly5, respectively. The lysostaphin immunity factor Lif was able to complement FemB, as could be shown by serine incorporation and by an increase in lysostaphin resistance in the wild-type as well as in a femB mutant. However, Lif could not substitute for FemA in femA or in femAB-null mutants. Methicillin resistance, which is dependent on functional FemA and FemB, was not complemented by Lif, suggesting that serine-substituted side chains are a lesser substrate for penicillin-binding protein PBP2' in methicillin resistance.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / analysis
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Bacterial Proteins / genetics
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Bacterial Proteins / physiology*
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Carrier Proteins*
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Cell Wall / chemistry
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Genetic Complementation Test
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Glycine / analysis
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Glycine / metabolism
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Hexosyltransferases / metabolism
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Lysostaphin
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Methicillin Resistance
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Multienzyme Complexes / metabolism
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Muramoylpentapeptide Carboxypeptidase*
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Mutation
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Penicillin-Binding Proteins
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Peptidoglycan / biosynthesis
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Peptidoglycan / chemistry*
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Peptidyl Transferases / metabolism
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Serine / analysis
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Staphylococcus aureus / metabolism*
Substances
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Amino Acids
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Bacterial Proteins
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Carrier Proteins
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FemA protein, Bacteria
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FemB protein, Staphylococcus epidermidis
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Multienzyme Complexes
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Penicillin-Binding Proteins
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Peptidoglycan
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Serine
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Peptidyl Transferases
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Hexosyltransferases
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Muramoylpentapeptide Carboxypeptidase
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Lysostaphin
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Glycine