Early midcell localization of Escherichia coli PBP4 supports the function of peptidoglycan amidases.

Autor: Verheul J; Bacterial Cell Biology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands., Lodge A; Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom., Yau HCL; Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom., Liu X; Bacterial Cell Biology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands.; Department of Biochemistry, University of Oxford, Oxford, United Kingdom., Boelter G; Institute of Microbiology & Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom., Liu X; Bacterial Cell Biology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands., Solovyova AS; NUPPA, Leech Building, Framlington Place, Newcastle upon Tyne, United Kingdom., Typas A; European Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.; European Molecular Biology Laboratory, Structural & Computational Unit, Heidelberg, Germany., Banzhaf M; Institute of Microbiology & Infection and School of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom., Vollmer W; Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom., den Blaauwen T; Bacterial Cell Biology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands.
Jazyk: angličtina
Zdroj: PLoS genetics [PLoS Genet] 2022 May 23; Vol. 18 (5), pp. e1010222. Date of Electronic Publication: 2022 May 23 (Print Publication: 2022).
DOI: 10.1371/journal.pgen.1010222
Abstrakt: Insertion of new material into the Escherichia coli peptidoglycan (PG) sacculus between the cytoplasmic membrane and the outer membrane requires a well-organized balance between synthetic and hydrolytic activities to maintain cell shape and avoid lysis. Since most bacteria carry multiple enzymes carrying the same type of PG hydrolytic activity, we know little about the specific function of given enzymes. Here we show that the DD-carboxy/endopeptidase PBP4 localizes in a PBP1A/LpoA and FtsEX dependent fashion at midcell during septal PG synthesis. Midcell localization of PBP4 requires its non-catalytic domain 3 of unknown function, but not the activity of PBP4 or FtsE. Microscale thermophoresis with isolated proteins shows that PBP4 interacts with NlpI and the FtsEX-interacting protein EnvC, an activator of amidases AmiA and AmiB, which are needed to generate denuded glycan strands to recruit the initiator of septal PG synthesis, FtsN. The domain 3 of PBP4 is needed for the interaction with NlpI and EnvC, but not PBP1A or LpoA. In vivo crosslinking experiments confirm the interaction of PBP4 with PBP1A and LpoA. We propose that the interaction of PBP4 with EnvC, whilst not absolutely necessary for mid-cell recruitment of either protein, coordinates the activities of PBP4 and the amidases, which affects the formation of denuded glycan strands that attract FtsN. Consistent with this model, we found that the divisome assembly at midcell was premature in cells lacking PBP4, illustrating how the complexity of interactions affect the timing of cell division initiation.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
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