Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora

Botanical Studies
Luyi JiangZhi Hong

Abstract

Asparagine (N)-linked glycosylation is one of the most crucial post-translational modifications, which is catalyzed in the lumen of the endoplasmic reticulum (ER) by the oligosaccharyltransferase (OST) in eukaryotic cells. Biochemical and genetic assay leads to the identification of the nine subunits (Ost 1-6, Stt3, Swp1 and Wbp1) of the yeast OST and in which Stt3p is proposed playing a central and conserved role in N-glycosylation. Two STT3 isoform genes, STT3A and STT3B, exist in the plant and mammal genomes. OST with different catalytic STT3 isoforms has different enzymatic properties in mammals. The mutation of STT3A in Arabidopsis thaliana causes a salt hypersensitive phenotype the inhibited root growth and swollen root tips suggesting protein N-glycosylation is indispensable for plant growth and development. Spartina alterniflora is widely used for shoreline protection and tidal marsh restoration due to the strong salt tolerance although the exact molecular mechanism is little known. To explore the possible biological roles of N-glycosylation in plant adaptive resistance to salinity stress, we cloned the STT3 genes from S. alterniflora and heterogenously expressed them in Arabidopsis mutant to observe the functional cons...Continue Reading

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Citations

May 24, 2021·The Journal of Biological Chemistry·Jillianne EyringMarkus Aebi

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Methods Mentioned

BETA
transgenic
glycosylation
protein folding
electrophoresis
PCR
Fluorescence

Software Mentioned

TOPO2
ClustalW2
MEGA
ExPASy
TMpred
NetNGlyc

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