ActS activates peptidoglycan amidases during outer membrane stress in Escherichia coli.
Bacterial Outer Membrane
/ physiology
Carboxypeptidases
/ genetics
Cell Membrane
/ physiology
Cell Wall
/ metabolism
Endopeptidases
/ genetics
Escherichia coli
/ genetics
Escherichia coli Proteins
/ metabolism
Gene Deletion
Lipopolysaccharides
/ metabolism
N-Acetylmuramoyl-L-alanine Amidase
/ genetics
Penicillin-Binding Proteins
/ metabolism
Peptidoglycan
/ metabolism
Peptidoglycan Glycosyltransferase
/ metabolism
Plasmids
/ genetics
Serine-Type D-Ala-D-Ala Carboxypeptidase
/ metabolism
Stress, Physiological
/ physiology
Escherichia coli
cell division
cell envelope
lipopolysaccharide
peptidoglycan
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
07 2021
07 2021
Historique:
revised:
26
02
2021
received:
16
11
2020
accepted:
02
03
2021
pubmed:
5
3
2021
medline:
15
12
2021
entrez:
4
3
2021
Statut:
ppublish
Résumé
The integrity of the cell envelope of E. coli relies on the concerted activity of multi-protein machineries that synthesize the peptidoglycan (PG) and the outer membrane (OM). Our previous work found that the depletion of lipopolysaccharide (LPS) export to the OM induces an essential PG remodeling process involving LD-transpeptidases (LDTs), the glycosyltransferase function of PBP1B and the carboxypeptidase PBP6a. Consequently, cells with defective OM biogenesis lyse if they lack any of these PG enzymes. Here we report that the morphological defects, and lysis associated with a ldtF mutant with impaired LPS transport, are alleviated by the loss of the predicted OM-anchored lipoprotein ActS (formerly YgeR). We show that ActS is an inactive member of LytM-type peptidoglycan endopeptidases due to a degenerated catalytic domain. ActS is capable of activating all three main periplasmic peptidoglycan amidases, AmiA, AmiB, and AmiC, which were previously reported to be activated only by EnvC and/or NlpD. Our data also suggest that in vivo ActS preferentially activates AmiC and that its function is linked to cell envelope stress.
Identifiants
pubmed: 33660879
doi: 10.1111/mmi.14712
pmc: PMC8360153
doi:
Substances chimiques
Escherichia coli Proteins
0
Lipopolysaccharides
0
Penicillin-Binding Proteins
0
Peptidoglycan
0
peptidoglycan endopeptidase
0
Peptidoglycan Glycosyltransferase
EC 2.4.1.129
penicillin-binding protein 1B, E coli
EC 2.4.1.129
Carboxypeptidases
EC 3.4.-
Endopeptidases
EC 3.4.-
Serine-Type D-Ala-D-Ala Carboxypeptidase
EC 3.4.16.4
N-Acetylmuramoyl-L-alanine Amidase
EC 3.5.1.28
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
329-342Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/S010122/1
Pays : United Kingdom
Informations de copyright
© 2021 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
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