Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli |
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| Authors: | René van der Ploeg Jolanda Verheul Norbert O. E. Vischer Eelco Hoogendoorn Marten Postma Waldemar Vollmer Tanneke den Blaauwen |
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| Affiliation: | 1. Bacterial Cell Biology, Swammerdam Institute for Life Sciences, University of Amsterdam, , 1090 GE Amsterdam, the Netherlands;2. Molecular Cytology, Swammerdam Institute for Life Sciences, University of Amsterdam, , 1090 GE Amsterdam, the Netherlands;3. Institute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University, , Newcastle upon Tyne, NE2 4AX UK |
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| Abstract: | The rod‐shaped bacterium Escherichia coli grows by insertion of peptidoglycan into the lateral wall during cell elongation and synthesis of new poles during cell division. The monofunctional transpeptidases PBP2 and PBP3 are part of specialized protein complexes called elongasome and divisome, respectively, which catalyse peptidoglycan extension and maturation. Endogenous immunolabelled PBP2 localized in the cylindrical part of the cell as well as transiently at midcell. Using the novel image analysis tool Coli‐Inspector to analyse protein localization as function of the bacterial cell age, we compared PBP2 localization with that of other E. coli cell elongation and division proteins including PBP3. Interestingly, the midcell localization of the two transpeptidases overlaps in time during the early period of divisome maturation. Försters Resonance Energy Transfer (FRET) experiments revealed an interaction between PBP2 and PBP3 when both are present at midcell. A decrease in the midcell diameter is visible after 40% of the division cycle indicating that the onset of new cell pole synthesis starts much earlier than previously identified by visual inspection. The data support a new model of the division cycle in which the elongasome and divisome interact to prepare for cell division. |
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