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Lookup NU author(s): Dr Victor Hernandez-RocamoraORCiD, Marta Zaccaria, Professor Waldemar Vollmer
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2025 Hernández-Rocamora et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Peptidoglycan hydrolases facilitate bacterial cell wall growth by creating space for insertion of new material and allowing physical separation of daughter cells. In Escherichia coli, three peptidoglycan amidases, AmiA, AmiB and AmiC, cleave septal peptidoglycan during cell division. The LytM-domain proteins EnvC, NlpD and ActS activate these amidases either from inside the cell or the outer membrane: EnvC binds to the cytoplasmic membrane-anchored divisome components FtsEX, while NlpD and ActS are outer membrane-anchored lipoproteins. Here we report the identification of a novel periplasmic deacetylase called SddA that removes acetyl groups from denuded peptidoglycan glycan strands, the products of amidases. The sddA gene is co-expressed with the gene encoding EnvC, linking SddA function to amidase activation. Consistent with this link, the deletion of sddA alleviates phenotypes associated with lack of amidase activation, while overexpression of sddA alleviates phenotypes related to a defective Tol-Pal system and causes cell chaining due to reduced septum peptidoglycan cleavage. We present a model according to which SddA modulates the activation of the septum-splitting amidases during cell division.
Author(s): Hernandez-Rocamora VM, Martorana AM, Belloso A, Ballesteros D, Zaccaria M, Perez AJ, Iorga BI, Abia D, Gray J, Breukink E, Xiao J, Pazos M, Polissi A, Vollmer W
Publication type: Article
Publication status: Published
Journal: PLoS Genetics
Year: 2025
Volume: 21
Issue: 9
Online publication date: 05/09/2025
Acceptance date: 25/08/2025
Date deposited: 16/09/2025
ISSN (print): 1553-7390
ISSN (electronic): 1553-7404
Publisher: Public Library of Science
URL: https://doi.org/10.1371/journal.pgen.1011626
DOI: 10.1371/journal.pgen.1011626
Data Access Statement: All raw data are presented in the manuscript.
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