Arabidopsis thalianaalpha1,2‐glucosyltransferase (ALG10) is required for efficient N‐glycosylation and leaf growth
| العنوان: | Arabidopsis thalianaalpha1,2‐glucosyltransferase (ALG10) is required for efficient N‐glycosylation and leaf growth |
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| المؤلفون: | Josef Glössl, Jennifer Schoberer, Friedrich Altmann, Akhlaq Farid, Richard Strasser, Martin Pabst |
| المصدر: | The Plant Journal |
| بيانات النشر: | Wiley, 2011. |
| سنة النشر: | 2011 |
| مصطلحات موضوعية: | 0106 biological sciences, Glycosylation, Mutant, Arabidopsis, Oligosaccharides, Plant Science, Endoplasmic Reticulum, glycosyltransferase, 01 natural sciences, chemistry.chemical_compound, N-linked glycosylation, protein glycosylation, Arabidopsis thaliana, Asparagine, 2. Zero hunger, 0303 health sciences, biology, food and beverages, Salt Tolerance, lipid-linked oligosaccharides, Phenotype, Carbohydrate Sequence, Biochemistry, Glucosyltransferases, abiotic stress, Green Fluorescent Proteins, Molecular Sequence Data, Saccharomyces cerevisiae, 03 medical and health sciences, Polysaccharides, Stress, Physiological, Tobacco, Genetics, Polyisoprenyl Phosphate Sugars, 030304 developmental biology, posttranslational modification, Arabidopsis Proteins, Genetic Complementation Test, fungi, Original Articles, Cell Biology, biology.organism_classification, Plant Leaves, Mutagenesis, Insertional, chemistry, Unfolded Protein Response, Unfolded protein response, Protein Processing, Post-Translational, 010606 plant biology & botany |
| الوصف: | Assembly of the dolichol-linked oligosaccharide precursor (Glc(3) Man(9) GlcNAc(2) ) is highly conserved among eukaryotes. In contrast to yeast and mammals, little is known about the biosynthesis of dolichol-linked oligosaccharides and the transfer to asparagine residues of nascent polypeptides in plants. To understand the biological function of these processes in plants we characterized the Arabidopsis thaliana homolog of yeast ALG10, the α1,2-glucosyltransferase that transfers the terminal glucose residue to the lipid-linked precursor. Expression of an Arabidopsis ALG10-GFP fusion protein in Nicotiana benthamiana leaf epidermal cells revealed a reticular distribution pattern resembling endoplasmic reticulum (ER) localization. Analysis of lipid-linked oligosaccharides showed that Arabidopsis ALG10 can complement the yeast Δalg10 mutant strain. A homozygous Arabidopsis T-DNA insertion mutant (alg10-1) accumulated mainly lipid-linked Glc(2) Man(9) GlcNAc(2) and displayed a severe protein underglycosylation defect. Phenotypic analysis of alg10-1 showed that mutant plants have altered leaf size when grown in soil. Moreover, the inactivation of ALG10 in Arabidopsis resulted in the activation of the unfolded protein response, increased salt sensitivity and suppression of the phenotype of α-glucosidase I-deficient plants. In summary, these data show that Arabidopsis ALG10 is an ER-resident α1,2-glucosyltransferase that is required for lipid-linked oligosaccharide biosynthesis and subsequently for normal leaf development and abiotic stress response. |
| تدمد: | 1365-313X 0960-7412 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46696d3f5217972881a00f5fd7d5a9b6 https://doi.org/10.1111/j.1365-313x.2011.04688.x |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....46696d3f5217972881a00f5fd7d5a9b6 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1365313X 09607412 |
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