Staphylococcus aureus sacculus mediates activities of M23 hydrolases.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
23 10 2023
Historique:
received: 13 04 2023
accepted: 12 10 2023
medline: 27 10 2023
pubmed: 24 10 2023
entrez: 23 10 2023
Statut: epublish

Résumé

Peptidoglycan, a gigadalton polymer, functions as the scaffold for bacterial cell walls and provides cell integrity. Peptidoglycan is remodelled by a large and diverse group of peptidoglycan hydrolases, which control bacterial cell growth and division. Over the years, many studies have focused on these enzymes, but knowledge on their action within peptidoglycan mesh from a molecular basis is scarce. Here, we provide structural insights into the interaction between short peptidoglycan fragments and the entire sacculus with two evolutionarily related peptidases of the M23 family, lysostaphin and LytM. Through nuclear magnetic resonance, mass spectrometry, information-driven modelling, site-directed mutagenesis and biochemical approaches, we propose a model in which peptidoglycan cross-linking affects the activity, selectivity and specificity of these two structurally related enzymes differently.

Identifiants

pubmed: 37872144
doi: 10.1038/s41467-023-42506-w
pii: 10.1038/s41467-023-42506-w
pmc: PMC10593780
doi:

Substances chimiques

Peptidoglycan 0
Hydrolases EC 3.-
Lysostaphin EC 3.4.24.75

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

6706

Informations de copyright

© 2023. Springer Nature Limited.

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Auteurs

Alicja Razew (A)

Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 71 avenue des Martyrs-CS10090, Grenoble cedex 9, 38044, France.
International Institute of Molecular and Cell Biology in Warsaw, 4 Ks. Trojdena Street, 02-109, Warsaw, Poland.
Laboratory of Protein Engineering, Mossakowski Medical Research Institute, Polish Academy of Sciences, 5 Pawinskiego Street, 02-106, Warsaw, Poland.

Cedric Laguri (C)

Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 71 avenue des Martyrs-CS10090, Grenoble cedex 9, 38044, France.

Alicia Vallet (A)

Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 71 avenue des Martyrs-CS10090, Grenoble cedex 9, 38044, France.

Catherine Bougault (C)

Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 71 avenue des Martyrs-CS10090, Grenoble cedex 9, 38044, France.

Magdalena Kaus-Drobek (M)

Laboratory of Protein Engineering, Mossakowski Medical Research Institute, Polish Academy of Sciences, 5 Pawinskiego Street, 02-106, Warsaw, Poland.

Izabela Sabala (I)

International Institute of Molecular and Cell Biology in Warsaw, 4 Ks. Trojdena Street, 02-109, Warsaw, Poland. isabala@imdik.pan.pl.
Laboratory of Protein Engineering, Mossakowski Medical Research Institute, Polish Academy of Sciences, 5 Pawinskiego Street, 02-106, Warsaw, Poland. isabala@imdik.pan.pl.

Jean-Pierre Simorre (JP)

Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 71 avenue des Martyrs-CS10090, Grenoble cedex 9, 38044, France. jean-pierre.simorre@ibs.fr.

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Classifications MeSH