Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
07 09 2021
07 09 2021
Historique:
received:
20
04
2021
accepted:
23
08
2021
entrez:
8
9
2021
pubmed:
9
9
2021
medline:
15
12
2021
Statut:
epublish
Résumé
Glycosylation is increasingly recognised as a common protein modification within bacterial proteomes. While great strides have been made in identifying species that contain glycosylation systems, our understanding of the proteins and sites targeted by these systems is far more limited. Within this work we explore the conservation of glycoproteins and glycosylation sites across the pan-Burkholderia glycoproteome. Using a multi-protease glycoproteomic approach, we generate high-confidence glycoproteomes in two widely utilized B. cenocepacia strains, K56-2 and H111. This resource reveals glycosylation occurs exclusively at Serine residues and that glycoproteins/glycosylation sites are highly conserved across B. cenocepacia isolates. This preference for glycosylation at Serine residues is observed across at least 9 Burkholderia glycoproteomes, supporting that Serine is the dominant residue targeted by PglL-mediated glycosylation across the Burkholderia genus. Combined, this work demonstrates that PglL enzymes of the Burkholderia genus are Serine-preferring oligosaccharyltransferases that target conserved and shared protein substrates.
Identifiants
pubmed: 34493791
doi: 10.1038/s42003-021-02588-y
pii: 10.1038/s42003-021-02588-y
pmc: PMC8423747
doi:
Substances chimiques
Bacterial Proteins
0
Glycoproteins
0
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1045Subventions
Organisme : Department of Education and Training | Australian Research Council (ARC)
ID : DP210100362
Organisme : Department of Education and Training | Australian Research Council (ARC)
ID : FT200100270
Informations de copyright
© 2021. The Author(s).
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