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Cell Division Inhibition in Salmonella typhimurium Histidine-Constitutive Strains: an ftsI-Like Defect in the Presence of Wild-Type Penicillin-Binding Protein 3 Levels

 

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Opened Access Cell Division Inhibition in Salmonella typhimurium Histidine-Constitutive Strains: an ftsI-Like Defect in the Presence of Wild-Type Penicillin-Binding Protein 3 Levels
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Author: Cano González, David A.
Mouslim, Chakib
Ayala, Juan A.
García del Portillo, Francisco
Casadesús Pursals, Josep
Department: Universidad de Sevilla. Departamento de Genética
Date: 1998
Published in: Journal of Bacteriology, 180 (19), 5231-5234.
Document type: Article
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.
Cite: Cano González, D.A., Mouslim, C., Ayala, J.A., García del Portillo, F. y Casadesús Pursals, J. (1998). Cell Division Inhibition in Salmonella typhimurium Histidine-Constitutive Strains: an ftsI-Like Defect in the Presence of Wild-Type Penicillin-Binding Protein 3 Levels. Journal of Bacteriology, 180 (19), 5231-5234.
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URI: https://hdl.handle.net/11441/79468

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