Advanced glycation end-product crosslinking activates a type VI secretion system phospholipase effector protein.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
11 Oct 2024
11 Oct 2024
Historique:
received:
09
04
2024
accepted:
01
10
2024
medline:
12
10
2024
pubmed:
12
10
2024
entrez:
11
10
2024
Statut:
epublish
Résumé
Advanced glycation end-products (AGE) are a pervasive form of protein damage implicated in the pathogenesis of neurodegenerative disease, atherosclerosis and diabetes mellitus. Glycation is typically mediated by reactive dicarbonyl compounds that accumulate in all cells as toxic byproducts of glucose metabolism. Here, we show that AGE crosslinking is harnessed to activate an antibacterial phospholipase effector protein deployed by the type VI secretion system of Enterobacter cloacae. Endogenous methylglyoxal reacts with a specific arginine-lysine pair to tether the N- and C-terminal α-helices of the phospholipase domain. Substitutions at these positions abrogate both crosslinking and toxic phospholipase activity, but in vitro enzyme function can be restored with an engineered disulfide that covalently links the N- and C-termini. Thus, AGE crosslinking serves as a bona fide post-translation modification to stabilize phospholipase structure. Given the ubiquity of methylglyoxal in prokaryotic and eukaryotic cells, these findings suggest that glycation may be exploited more generally to stabilize other proteins. This alternative strategy to fortify tertiary structure could be particularly advantageous in the cytoplasm, where redox potentials preclude disulfide bond formation.
Identifiants
pubmed: 39394186
doi: 10.1038/s41467-024-53075-x
pii: 10.1038/s41467-024-53075-x
doi:
Substances chimiques
Glycation End Products, Advanced
0
Bacterial Proteins
0
Pyruvaldehyde
722KLD7415
Arginine
94ZLA3W45F
Lysine
K3Z4F929H6
Disulfides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
8804Subventions
Organisme : U.S. Department of Health & Human Services | National Institutes of Health (NIH)
ID : GM117930
Organisme : U.S. Department of Health & Human Services | National Institutes of Health (NIH)
ID : GM144437
Organisme : U.S. Department of Health & Human Services | National Institutes of Health (NIH)
ID : GM144437
Informations de copyright
© 2024. The Author(s).
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