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Role of endopeptidases in peptidoglycan synthesis mediated by alternative cross-linking enzymes in Escherichia coli

View ORCID ProfileHenri Voedts, Delphine Dorchêne, Adam Lodge, View ORCID ProfileWaldemar Vollmer, View ORCID ProfileMichel Arthur, View ORCID ProfileJean-Emmanuel Hugonnet
doi: https://doi.org/10.1101/2021.02.12.430937
Henri Voedts
aCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, F-75006 Paris, France
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  • ORCID record for Henri Voedts
Delphine Dorchêne
aCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, F-75006 Paris, France
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Adam Lodge
bCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK
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Waldemar Vollmer
bCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK
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Michel Arthur
aCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, F-75006 Paris, France
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  • For correspondence: michel.arthur@crc.jussieu.fr jean-emmanuel.hugonnet@crc.jussieu.fr
Jean-Emmanuel Hugonnet
aCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, F-75006 Paris, France
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  • For correspondence: michel.arthur@crc.jussieu.fr jean-emmanuel.hugonnet@crc.jussieu.fr
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ABSTRACT

Bacteria resist to the turgor pressure of the cytoplasm through a net-like macromolecule, the peptidoglycan, made of glycan strands connected via peptides cross-linked by penicillin-binding proteins (PBPs). We recently reported the emergence of β-lactam resistance resulting from a bypass of PBPs by the YcbB L,D-transpeptidase (LdtD), which form chemically distinct 3→3 cross-links compared to 4→3 formed by PBPs. Here we show that peptidoglycan expansion requires controlled hydrolysis of cross-links and identify amongst eight endopeptidase paralogues the minimum enzyme complements essential for bacterial growth with 4→3 (MepM) and 3→3 (MepM and MepK) cross-links. Purified Mep endopeptidases unexpectedly displayed a 4→3 and 3→3 dual specificity implying recognition of a common motif in the two cross-link types. Uncoupling of the polymerization of glycan chains from the 4→3 cross-linking reaction was found to facilitate the bypass of PBPs by YcbB. These results illustrate the plasticity of the peptidoglycan polymerization machinery in response to the selective pressure of β-lactams.

Competing Interest Statement

The authors have declared no competing interest.

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Posted February 25, 2021.
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Role of endopeptidases in peptidoglycan synthesis mediated by alternative cross-linking enzymes in Escherichia coli
Henri Voedts, Delphine Dorchêne, Adam Lodge, Waldemar Vollmer, Michel Arthur, Jean-Emmanuel Hugonnet
bioRxiv 2021.02.12.430937; doi: https://doi.org/10.1101/2021.02.12.430937
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Role of endopeptidases in peptidoglycan synthesis mediated by alternative cross-linking enzymes in Escherichia coli
Henri Voedts, Delphine Dorchêne, Adam Lodge, Waldemar Vollmer, Michel Arthur, Jean-Emmanuel Hugonnet
bioRxiv 2021.02.12.430937; doi: https://doi.org/10.1101/2021.02.12.430937

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