Arabidopsis thalianaalpha1,2‐glucosyltransferase (ALG10) is required for efficient N‐glycosylation and leaf growth

Autor: Josef Glössl, Jennifer Schoberer, Friedrich Altmann, Akhlaq Farid, Richard Strasser, Martin Pabst
Rok vydání: 2011
Předmět:
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
Zdroj: The Plant Journal
ISSN: 1365-313X
0960-7412
DOI: 10.1111/j.1365-313x.2011.04688.x
Popis: 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.
Databáze: OpenAIRE
Externí odkaz: