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• W4386001320 abstract "Abstract 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) 32 tag, consisting of 32 repeats of a Ser-Pro motif, in tobacco BY-2 cells. When cells were grown in MS medium, the (SP) 32 -EGFP formed protein body-like aggregate and was retained in the ER, without undergoing Hyp- O -glycosylation. In contrast, the fusion protein becomes fully Hyp- O -glycosylated, and then secreted in SH medium. Transcriptome analysis of the BY-2 cells grown in SH medium vs. MS medium revealed over 16,000 DEGs, with many upregulated DEGs associated with the microtubule-based movement, movement of subcellular component, and microtubule binding. These DEGs are presumably responsible for the enhanced ER-Golgi transport of HypGP-tagged proteins, enabling their glycosylation and secretion in SH medium." @default.
• W4386001320 created "2023-08-20" @default.
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• W4386001320 date "2023-08-19" @default.
• W4386001320 modified "2023-10-12" @default.
• W4386001320 title "Intracellular trafficking and glycosylation of hydroxyproline-O-glycosylation module in tobacco BY-2 cells is dependent on medium composition and transcriptome analysis" @default.
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• W4386001320 doi "https://doi.org/10.1038/s41598-023-40723-3" @default.
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