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Lookup NU author(s): Professor Waldemar Vollmer, Manuel Banzhaf
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2024 The Author(s). Molecular Microbiology published by John Wiley & Sons Ltd.Escherichia coli has many periplasmic hydrolases to degrade and modify peptidoglycan (PG). However, the redundancy of eight PG endopeptidases makes it challenging to define specific roles to individual enzymes. Therefore, the cellular role of PBP7 (encoded by pbpG) is not clearly defined. In this work, we show that PBP7 localizes in the lateral cell envelope and at midcell. The C-terminal α-helix of PBP7 is crucial for midcell localization but not for its activity, which is dispensable for this localization. Additionally, midcell localization of PBP7 relies on the assembly of FtsZ up to FtsN in the divisome, and on the activity of PBP3. PBP7 was found to affect the assembly timing of FtsZ and FtsN in the divisome. The absence of PBP7 slows down the assembly of FtsN at midcell. The ΔpbpG mutant exhibited a weaker incorporation of the fluorescent D-amino acid HADA, reporting on transpeptidase activity, compared to wild-type cells. This could indicate reduced PG synthesis at the septum of the ΔpbpG strain, explaining the slower accumulation of FtsN and suggesting that endopeptidase-mediated PG cleavage may be a rate-limiting step for septal PG synthesis.
Author(s): Liu X, Boelter G, Vollmer W, Banzhaf M, denBlaauwen T
Publication type: Article
Publication status: Published
Journal: Molecular Microbiology
Year: 2024
Pages: epub ahead of print
Online publication date: 30/09/2024
Acceptance date: 10/09/2024
Date deposited: 14/10/2024
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: John Wiley and Sons Inc
URL: https://doi.org/10.1111/mmi.15321
DOI: 10.1111/mmi.15321
Data Access Statement: All data are provided in this manuscript and in the supporting data.
PubMed id: 39344863
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