Mechanistic insights into Schizosaccharomyces pombe GT-A family protein Pvg3 in the biosynthesis of pyruvylated β1,3-galactose of N-linked oligosaccharides.
Fission yeast
GT-A family
Galactosyltransferase
N-glycan
Pyruvylated galactose
Journal
Journal of bioscience and bioengineering
ISSN: 1347-4421
Titre abrégé: J Biosci Bioeng
Pays: Japan
ID NLM: 100888800
Informations de publication
Date de publication:
Jun 2023
Jun 2023
Historique:
received:
09
01
2023
revised:
24
02
2023
accepted:
04
03
2023
medline:
29
5
2023
pubmed:
1
4
2023
entrez:
31
3
2023
Statut:
ppublish
Résumé
N-linked oligosaccharides in the fission yeast Schizosaccharomyces pombe contain large amounts of d-galactose (Gal), which mainly comprises α1,2- and α1,3-linked Gal except for pyruvylated β1,3-linked Gal (PvGalβ) at the non-reducing end. The PvGalβ unit of N-glycans is important for regulating nonsexual flocculation and invasive growth, but the mechanistic basis for β-galactosylation in fission yeast is poorly understood. To gain insight into this mechanism, we have characterized three genes previously identified to be involved in PvGalβ biosynthesis (pvg2, pvg3, and pvg5), with a focus on pvg3, which is predicted to contain a domain conserved in galactosyltransferase family 31 (GT31) proteins. Fluorescent microscopy revealed that Pvg3 is stably localized at the Golgi membrane, regardless of the presence of pvg2
Identifiants
pubmed: 37002018
pii: S1389-1723(23)00074-9
doi: 10.1016/j.jbiosc.2023.03.002
pii:
doi:
Substances chimiques
Galactose
X2RN3Q8DNE
Oligosaccharides
0
Polysaccharides
0
Galactosyltransferases
EC 2.4.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
423-432Informations de copyright
Copyright © 2023 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.