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Entry URI http://metadb.riken.jp/db/SciNetS_ria224i/cria224u4ria224u15860005i
Entry name Lerouxel Olivier et al. 2005 May. Plant J. 42(4):455-68.
Title Mutants in DEFECTIVE GLYCOSYLATION, an Arabidopsis homolog of an oligosaccharyltransferase complex subunit, show protein underglycosylation and defects in cell differentiation and growth.
Authors And竪me-Onzighi Christine|Bruyant Marie-Pierre|Driouich Azeddine|H旦fte Herman|Lerouge Patrice|Lerouxel Olivier|Loutelier-Bourhis Corinne|Mouille Gr辿gory|S辿veno Martial
Abstract A mutant called defective glycosylation1-1 (dgl1-1) was identified in Arabidopsis based on a growth defect of the dark-grown hypocotyl and an abnormal composition of the non-cellulosic cell wall polysaccharides. dgl1-1 is altered in a protein ortholog of human OST48 or yeast WBP1, an essential protein subunit of the oligosaccharyltransferase (OST) complex, which is responsible for the transfer in the ER of the N-linked glycan precursor onto Asn residues of candidate proteins. Consistent with the known function of the OST complex in eukaryotes, the dgl1-1 mutation led to a reduced N-linked glycosylation of the ER-resident protein disulfide isomerase. A second more severe mutant (dgl1-2) was embryo-lethal. Microscopic analysis of dgl1-1 revealed developmental defects including reduced cell elongation and the collapse and differentiation defects of cells in the central cylinder. These defects were accompanied by changes in the non-cellulosic polysaccharide composition, including the accumulation of ectopic callose. Interestingly, in contrast to other dwarf mutants that are altered in early steps of the N-glycan processing, dgl1-1 did not exhibit a cellulose deficiency. Together, these results confirm the role of DGL1 in N-linked glycosylation, cell growth and differentiation in plants.
Pubmed ID 15860005
Journal The Plant journal
Volume 42
Issue 4
Pages 455-68
Publication date 2005 May
Num of phenotype gene 0