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Fast lysis of Escherichia coli filament cells requires differentiation of potential division sites

Centro de Biología Molecular ‘Severo Ochoa’ Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid, Campus de Cantoblanco, 28049 Madrid, Spain¹
Max-Planck-Institut für Entwitcklungsbiologie, Spemannstrasse 35, D-72076 Tübingen, Germany²

Author for correspondence: Miguel Angel de Pedro. Tel: +34 91 3978083. Fax: +34 91 3978087. e-mail: madepedro{at}cbm.uam.es

Periodic activation of zonal peptidoglycan (murein) synthesis at division sites in Escherichia coli has been reported recently. Zonal synthesis is responsible for septum formation, whereas elongation of the cell sacculus is performed by diffuse insertion of precursors. Zonal synthesis can be triggered in ftsA, ftsQ and ftsI (pbpB) division mutants growing as filaments at the restrictive temperature, but not in ftsZ mutant strains. The lytic response to ß-lactams of cells able or unable to periodically trigger a zonal mode of murein synthesis could be substantially different. Therefore, we investigated the response to the bacteriolytic ß-lactam cefsulodin of ftsZ and ftsI mutants growing at the restrictive (42 °C) temperature. The ftsI cells lysed early and quickly after addition of the antibiotic. Sacculi of lysed cells were transversely cut in a very sharp way. In contrast the ftsZ strain lysed late and slowly after addition of the antibiotic and sacculi showed a generalized weakening of the murein network and extended breaks with a frayed appearance. No transversely cut sacculi comparable to those seen in the ftsI samples were found. Our results strongly support that ß-lactam-induced lysis occurs preferentially at division sites because of the activation of zonal murein synthesis at the initiation of septation.

Keywords: ftsZ, pbpB, penicillin-binding protein, beta-lactam, murein

Abbreviations: PBP, Penicillin-binding protein; SMS, septal murein synthesis

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