Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division

Manuel Pazos, Katharina Peters, Mercedes Casanova, Pilar Palacios, Michael VanNieuwenhze, Eefjan Breukink, Miguel Vicente and Waldemar Vollmer ()
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Manuel Pazos: Newcastle University
Katharina Peters: Newcastle University
Mercedes Casanova: Darwin 3
Pilar Palacios: Darwin 3
Michael VanNieuwenhze: Indiana University
Eefjan Breukink: Utrecht University
Miguel Vicente: Darwin 3
Waldemar Vollmer: Newcastle University

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract During the transition from elongation to septation, Escherichia coli establishes a ring-like peptidoglycan growth zone at the future division site. This preseptal peptidoglycan synthesis does not require the cell division-specific peptidoglycan transpeptidase PBP3 or most of the other cell division proteins, but it does require FtsZ, its membrane-anchor ZipA and at least one of the bi-functional transglycosylase-transpeptidases, PBP1A or PBP1B. Here we show that PBP1A and PBP1B interact with ZipA and localise to preseptal sites in cells with inhibited PBP3. ZipA stimulates the glycosyltransferase activity of PBP1A. The membrane-anchored cell division protein FtsN localises at preseptal sites and stimulates both activities of PBP1B. Genes zipA and ftsN can be individually deleted in ftsA* mutant cells, but the simultaneous depletion of both proteins is lethal and cells do not establish preseptal sites. Our data support a model according to which ZipA and FtsN-FtsA have semi-redundant roles in connecting the cytosolic FtsZ ring with the membrane-anchored peptidoglycan synthases during the preseptal phase of envelope growth.

Date: 2018
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DOI: 10.1038/s41467-018-07559-2

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