Mycobacterium smegmatis HtrA Blocks the Toxic Activity of a Putative Cell Wall Amidase.
Bacterial Proteins
/ chemistry
Glycosylation
Heat-Shock Proteins
/ chemistry
Lipoproteins
/ chemistry
Mannosyltransferases
/ genetics
Muramidase
/ genetics
Mutagenesis, Site-Directed
Mycobacterium smegmatis
/ growth & development
N-Acetylmuramoyl-L-alanine Amidase
/ genetics
PDZ Domains
Periplasmic Proteins
/ chemistry
Serine Endopeptidases
/ chemistry
Ami3
DegP
HtrA
Mycobacterium smegmatis
Mycobacterium tuberculosis
N-acetylmuramoyl-L-alanine amidase
Pmt
mannosyltransferase
protease
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
21 05 2019
21 05 2019
Historique:
received:
02
05
2018
revised:
14
10
2018
accepted:
13
12
2018
entrez:
23
5
2019
pubmed:
23
5
2019
medline:
9
7
2020
Statut:
ppublish
Résumé
Mycobacterium tuberculosis, the causative agent of tuberculosis, withstands diverse environmental stresses in the host. The periplasmic protease HtrA is required only to survive extreme conditions in most bacteria but is predicted to be essential for normal growth in mycobacteria. We confirm that HtrA is indeed essential in Mycobacterium smegmatis and interacts with another essential protein of unknown function, LppZ. However, the loss of any of three unlinked genes, including those encoding Ami3, a peptidoglycan muramidase, and Pmt, a mannosyltransferase, suppresses the essentiality of both HtrA and LppZ, indicating the functional relevance of these genes' protein products. Our data indicate that HtrA-LppZ is required to counteract the accumulation of active Ami3, which is toxic under the stabilizing influence of Pmt-based mannosylation. This suggests that HtrA-LppZ blocks the toxicity of a cell wall enzyme to maintain mycobacterial homeostasis.
Identifiants
pubmed: 31116989
pii: S2211-1247(18)32008-4
doi: 10.1016/j.celrep.2018.12.063
pmc: PMC6538288
mid: NIHMS1530009
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Heat-Shock Proteins
0
Lipoproteins
0
Periplasmic Proteins
0
Mannosyltransferases
EC 2.4.1.-
Muramidase
EC 3.2.1.17
DegP protease
EC 3.4.21.-
Serine Endopeptidases
EC 3.4.21.-
EJL amidase
EC 3.5.1.-
N-Acetylmuramoyl-L-alanine Amidase
EC 3.5.1.28
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
2468-2479.e3Subventions
Organisme : NIAID NIH HHS
ID : F31 AI131502
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI107774
Pays : United States
Informations de copyright
Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.
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