Abstract
Histidine-constitutive (Hisc) strains of Salmonella typhimurium undergo cell division inhibition in the presence of high concentrations of a metabolizable carbon source. Filaments formed by Hisc strains show constrictions and contain evenly spaced nucleoids, suggesting a defect in septum formation. Inhibitors of penicillin-binding protein 3 (PBP3) induce a filamentation pattern identical to that of Hisc strains. However, the Hisc septation defect is caused neither by reduced PBP3 synthesis nor by reduced PBP3 activity. Gross modifications of peptidoglycan composition are also ruled out. D-Cycloserine, an inhibitor of the soluble pathway producing peptidoglycan precursors, causes phenotypic suppression of filamentation, suggesting that the septation defect of Hisc strains may be caused by scarcity of PBP3 substrate.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aztreonam / pharmacology
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Bacterial Proteins*
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Carrier Proteins*
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Cell Division
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Cycloserine / pharmacology
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Hexosyltransferases / antagonists & inhibitors
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Hexosyltransferases / biosynthesis
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Hexosyltransferases / physiology*
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Histidine*
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Monobactams / pharmacology
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Multienzyme Complexes / antagonists & inhibitors
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Multienzyme Complexes / biosynthesis
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Multienzyme Complexes / physiology*
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Muramoylpentapeptide Carboxypeptidase*
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Penicillin-Binding Proteins
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Peptidoglycan / analysis
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Peptidyl Transferases / antagonists & inhibitors
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Peptidyl Transferases / biosynthesis
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Peptidyl Transferases / physiology*
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Phenotype
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Salmonella typhimurium / cytology*
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Transaminases / genetics
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Transaminases / physiology
Substances
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Bacterial Proteins
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Carrier Proteins
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Monobactams
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Multienzyme Complexes
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Penicillin-Binding Proteins
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Peptidoglycan
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Histidine
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Cycloserine
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Peptidyl Transferases
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Hexosyltransferases
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Transaminases
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histidinol-phosphate aminotransferase
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Muramoylpentapeptide Carboxypeptidase
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Aztreonam