Intracellular trafficking and glycosylation of hydroxyproline-O-glycosylation module in tobacco BY-2 cells is dependent on medium composition and transcriptome analysis.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
19 08 2023
19 08 2023
Historique:
received:
10
04
2023
accepted:
16
08
2023
medline:
21
8
2023
pubmed:
20
8
2023
entrez:
19
8
2023
Statut:
epublish
Résumé
Expression of recombinant proteins in plant cells with a "designer" hydroxyproline (Hyp)-O-glycosylated peptide (HypGP), such as tandem repeats of a "Ser-Pro" motif, has been shown to boost the secreted protein yields. However, dramatic secretion and Hyp-O-glycosylation of HypGP-tagged proteins can only be achieved when the plant cells were grown in nitrogen-deficient SH medium. Only trace amounts of secreted fusion protein were detected in MS medium. This study aims to gain a deeper understanding of the possible mechanism underlying these results by examining the intracellular trafficking and Hyp-O-glycosylation of enhanced green fluorescent protein (EGFP) fused with a (SP)
Identifiants
pubmed: 37598266
doi: 10.1038/s41598-023-40723-3
pii: 10.1038/s41598-023-40723-3
pmc: PMC10439957
doi:
Substances chimiques
Hydroxyproline
RMB44WO89X
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
13506Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM103429
Pays : United States
Organisme : NIDDK NIH HHS
ID : R15 DK128757
Pays : United States
Informations de copyright
© 2023. Springer Nature Limited.
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