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

BACKGROUND: 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...

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Autores principales: Jiang, Luyi, Zhu, Xin, Chen, Jinmei, Yang, Deyue, Zhou, Changfang, Hong, Zhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5432937/
https://www.ncbi.nlm.nih.gov/pubmed/28510840
http://dx.doi.org/10.1186/s40529-015-0111-9
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author Jiang, Luyi
Zhu, Xin
Chen, Jinmei
Yang, Deyue
Zhou, Changfang
Hong, Zhi
author_facet Jiang, Luyi
Zhu, Xin
Chen, Jinmei
Yang, Deyue
Zhou, Changfang
Hong, Zhi
author_sort Jiang, Luyi
collection PubMed
description BACKGROUND: 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 conservation. RESULTS: SaSTT3A 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 Arabidopsis stt3a-2 mutant salt-sensitive phenotype, indicating STT3A functions conservatively between glycophyte and halophyte and N-glycosylation might be involved in plant resistance to salinity. CONCLUSIONS: Two 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The 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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spelling pubmed-54329372017-05-31 Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora Jiang, Luyi Zhu, Xin Chen, Jinmei Yang, Deyue Zhou, Changfang Hong, Zhi Bot Stud Original Article BACKGROUND: 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 conservation. RESULTS: SaSTT3A 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 Arabidopsis stt3a-2 mutant salt-sensitive phenotype, indicating STT3A functions conservatively between glycophyte and halophyte and N-glycosylation might be involved in plant resistance to salinity. CONCLUSIONS: Two 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s40529-015-0111-9) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2015-11-11 /pmc/articles/PMC5432937/ /pubmed/28510840 http://dx.doi.org/10.1186/s40529-015-0111-9 Text en © Jiang et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Jiang, Luyi
Zhu, Xin
Chen, Jinmei
Yang, Deyue
Zhou, Changfang
Hong, Zhi
Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora
title Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora
title_full Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora
title_fullStr Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora
title_full_unstemmed Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora
title_short Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora
title_sort two conserved oligosaccharyltransferase catalytic subunits required for n-glycosylation exist in spartina alterniflora
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5432937/
https://www.ncbi.nlm.nih.gov/pubmed/28510840
http://dx.doi.org/10.1186/s40529-015-0111-9
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