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Journal of Bacteriology, October 1998, p. 5231-5234, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

David A. Cano,1 Chakib Mouslim,1 Juan A. Ayala,2 Francisco García-del Portillo,2 and Josep Casadesús1,*

Departamento de Genética, Facultad de Biología, Universidad de Sevilla, Seville 41080,1 and Centro de Biología Molecular Severo Ochoa, CSIC-Universidad Autónoma de Madrid, Cantoblanco, Madrid 28049,2 Spain

Received 6 April 1998/Accepted 11 July 1998

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.

* Corresponding author. Mailing address: Departamento de Genética, Facultad de Biología, Universidad de Sevilla, Apartado 1095, Seville 41080, Spain. Phone: 34 95 455 7105. Fax: 34 95 455 7104. E-mail: genbac{at}cica.es.

Journal of Bacteriology, October 1998, p. 5231-5234, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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