A protein O-GlcNAc glycosyltransferase regulates the antioxidative response in Yersinia pestis.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
16 Aug 2024
16 Aug 2024
Historique:
received:
11
07
2023
accepted:
23
07
2024
medline:
17
8
2024
pubmed:
17
8
2024
entrez:
16
8
2024
Statut:
epublish
Résumé
Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to proteins is commonly associated with a variety of stress responses and cellular processes in eukaryotes, but its potential roles in bacteria are unclear. Here, we show that protein HmwC acts as an O-GlcNAc transferase (OGT) responsible for O-GlcNAcylation of multiple proteins in Yersinia pestis, a flea-borne pathogen responsible for plague. We identify 64 O-GlcNAcylated proteins (comprising 65 sites) with differential abundance under conditions mimicking the mammalian host (Mh) and flea vector (Fv) environments. Deletion of hmwC, encoding a putative OGT, structurally distinct from any existing member of the GT41 family, results in reduced O-GlcNAcylation, reduced growth, and alterations in virulence properties and survival under stress. Purified HmwC can modify target proteins in vitro using UDP-GlcNAc as sugar donor. One of the target proteins, OsdY, promotes Y. pestis survival under oxidative stress conditions. Thus, our results support that regulation of antioxidative responses through O-GlcNAcylation may be a conserved process shared by prokaryotes and eukaryotes.
Identifiants
pubmed: 39152136
doi: 10.1038/s41467-024-50959-w
pii: 10.1038/s41467-024-50959-w
doi:
Substances chimiques
Bacterial Proteins
0
N-Acetylglucosaminyltransferases
EC 2.4.1.-
Acetylglucosamine
V956696549
O-GlcNAc transferase
EC 2.4.1.-
Antioxidants
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7062Informations de copyright
© 2024. The Author(s).
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