Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alternifloraReport as inadecuate

Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora - Download this document for free, or read online. Document in PDF available to download.

Botanical Studies

, 56:31



BackgroundAsparagine 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 conservation.

ResultsSaSTT3A and SaSTT3B genes were cloned from Spartina alterniflora. SaSTT3A genomic sequences spanned over 23 exons and 22 introns, while SaSTT3B had 6 exons and 5 introns. The gene structures of both genes were conserved among the analyzed plant species. Subcellular localization and transmembrane structure prediction revealed that these two genes had 13 and 11 transmembrane helices respectively. The functional complementation in which the cDNA of SaSTT3A and SaSTT3B driven by CaMV 35S promoter completely or partially rescued Arabidopsisstt3a-2 mutant salt-sensitive phenotype, indicating STT3A functions conservatively between glycophyte and halophyte and N-glycosylation might be involved in plant resistance to salinity.

ConclusionsTwo STT3 isoform genes, SaSTT3A and SaSTT3B, were cloned from S. alterniflora and they were evolutionally conserved at gene structure and coding sequences compared with their counterparts. Moreover, SaSTT3 genes could successfully rescue Arabidopsis stt3a-2 salt-sensitive phenotype, suggesting there exists a similar N-glycosylation process in S. alterniflora. Here we provided a first piece of evidence that the N-glycosylation might be involved in salt tolerance of halophyte.

KeywordsN-glycosylation STT3A Salt tolerance Spartina alterniflora Luyi Jiang and Xin Zhu contributed equally to this work

Electronic supplementary materialThe online version of this article doi:10.1186-s40529-015-0111-9 contains supplementary material, which is available to authorized users.

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Author: Luyi Jiang - Xin Zhu - Jinmei Chen - Deyue Yang - Changfang Zhou - Zhi Hong


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