Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
02 09 2023
02 09 2023
Historique:
received:
01
04
2022
accepted:
21
08
2023
medline:
4
9
2023
pubmed:
3
9
2023
entrez:
2
9
2023
Statut:
epublish
Résumé
Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion. However, the mechanisms of their coordination remain elusive. Moenomycin that inhibits a family of PG synthases known as Class-A penicillin-binding proteins (aPBPs), collapses rod shape despite aPBPs being non-essential for rod-like morphology in the bacterium Myxococcus xanthus. Here, we demonstrate that inhibited PBP1a2, an aPBP, accelerates the degradation of cell poles by DacB, a hydrolytic PG peptidase. Moenomycin promotes the binding between DacB and PG and thus reduces the mobility of DacB through PBP1a2. Conversely, DacB also regulates the distribution and dynamics of aPBPs. Our findings clarify the action of moenomycin and suggest that disrupting the coordination between PG synthases and hydrolases could be more lethal than eliminating individual enzymes.
Identifiants
pubmed: 37660104
doi: 10.1038/s41467-023-41082-3
pii: 10.1038/s41467-023-41082-3
pmc: PMC10475089
doi:
Substances chimiques
Peptidoglycan
0
Bambermycins
11015-37-5
Nitric Oxide Synthase
EC 1.14.13.39
Peptide Hydrolases
EC 3.4.-
Penicillin-Binding Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
5357Informations de copyright
© 2023. Springer Nature Limited.
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