Show legend Show as text

Structure type: polymer chemical repeating unit ; 25950
Compound class: fucoxylogalactan
Contained glycoepitopes: IEDB_136045,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142489,IEDB_144562,IEDB_151528,IEDB_152214,IEDB_174333,IEDB_190606,SB_36,SB_7,SB_86

• Article ID: 8599
  Chang CC, Cheng JJ, Lee IJ, Lu MK "Purification, structural elucidation, and anti-inflammatory activity of xylosyl galactofucan from Armillaria mellea" - Carbohydrate Polymers 114 (2018) 584-591
  

  A xylosyl 1,3-galactofucan (AMPS-III) was isolated and identified as a novel anti-inflammatory agent from an edible fungus, Armillaria mellea. The characteristics chemical structure of AMPS-III including the linkages of compositional monosaccharides and structure of the repeat unit were depicted and elucidated by proton, carbon and two-dimensional nuclear magnetic resonance techniques. AMPS-III was chemically proposed to have a partial 4-O-xylosylated 1,3-linked α-D-galactosyl-interlaced α-L-fucan composed of a pentadecasaccharide repeat unit with a molecular mass approximately 13 kDa. AMPS-III significantly suppressed the release of tumor necrosis factor-α (TNF-α) and cytokine monocyte chemotactic protein-1 (MCP-1) in RAW264.7 macrophages and EAhy926 following LPS and TNF-α induction. The results provide helpful evidences for application of AMPS-III as anti-inflammatory food supplements.

  polysaccharides, Armillaria mellea, anti-inflammation, galactofucan

  NCBI PubMed ID: 29452183
  Publication DOI: 10.1016/j.ijbiomac.2018.02.033
  Journal NLM ID: 8307156
  Publisher: Elsevier
  Correspondence: Chang CC ; Lu MK
  Institutions: Graduate Institute of Pharmacognosy, Taipei Medical University, Taipei, China, School of Pharmacy, College of Medicine, National Taiwan University, Taipei, China, National Research Institute of Chinese Medicine, Ministry of Health and Welfare, Taipei, China
  Methods: 13C NMR, 1H NMR, HPSEC, statistical analysis, TOCSY, cytokine production, phenol-sulfuric acid assay, DQF-COSY, HMBC, centrifugation, NOESY, HSQC, TFA hydrolysis
  
   
  
  Armillaria mellea
  CSDB ID 48820 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_115136,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_1394181,IEDB_140630,IEDB_141794,IEDB_142489,IEDB_144562,IEDB_149135,IEDB_151528,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_225177,IEDB_423153,IEDB_885823,SB_7,SB_86

• Article ID: 10073
  Stevenson TT, Darvill AG, Albersheim P "Structure of plant cell walls XXIII. Structural features of the plant cell-wall polysaccharide rhamnogalacturonan-II" - Carbohydrate Research 182 (1988) 207-226
  

  Rhamnogalacturonan-II (RG-II), isolated from the cell walls of suspension-cultured sycamore cells, has been further characterized. End-group analysis of RG-II showed that the polysaccharide contains about 30 glycosyl residues. Some 28 residues have been found as constituents of well characterized oligosaccharide fragments of RG-II. RG-II was treated with lithium metal dissolved in ethylenediamine to degrade the glycosyluronic acid residues. The major product was isolated, characterized, and shown to be the triglycosylalditol α-Xyl-(1→3)-α-Fuc-(1→4)-β-Rha-(1→31)-apiitol. This tetrasaccharide fragment of RG-II has three residues in common with a previously characterized heptasaccharide that had been derived from RG-II by partial hydrolysis with acid. RG-II was found to contain a large number of branched galactosyluronic acid residues that have not yet been identified as components of oligosaccharide fragments, although they are undoubtedly part of an octa(galactosyluronic acid) fragment generated by partial acid hydrolysis. The results of sequential partial acid hydrolysis provided evidence that, in RG-II, the extremely acid-labile 3-deoxy-d-manno-2-octulosonic-acid and 3-deoxy-d-lyxo-2-heptulosaric acid residues are attached to O-3 of 3,4-linked galactosyluronic acid residues, and that the mildly acid-labile apiofuranosyl residues are attached to O-2 of 2,4-linked galactosyluronic acid residues. These and previously published data suggested that RG-II has a highly branched structure, arranged around an α-(1→4)-linked galactosyluronic acid backbone.

  Publication DOI: 10.1016/0008-6215(88)84004-7
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Complex Carbohydrate Research Center and Department of Biochemistry, University of Georgia, Russell Research Center of the United States Department of Agriculture, Athens, Georgia, U.S.A.
  Methods: 1H NMR, gel filtration, FAB-MS, partial acid hydrolysis, GC-MS, acid hydrolysis
  
   
  
  Acer pseudoplatanus
  CSDB ID 115517 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_130699,IEDB_136045,IEDB_1394181,IEDB_142489,IEDB_144562,IEDB_149135,IEDB_152214,IEDB_174333,IEDB_225177,IEDB_885823,SB_86

• Article ID: 10073
  Stevenson TT, Darvill AG, Albersheim P "Structure of plant cell walls XXIII. Structural features of the plant cell-wall polysaccharide rhamnogalacturonan-II" - Carbohydrate Research 182 (1988) 207-226
  

  Rhamnogalacturonan-II (RG-II), isolated from the cell walls of suspension-cultured sycamore cells, has been further characterized. End-group analysis of RG-II showed that the polysaccharide contains about 30 glycosyl residues. Some 28 residues have been found as constituents of well characterized oligosaccharide fragments of RG-II. RG-II was treated with lithium metal dissolved in ethylenediamine to degrade the glycosyluronic acid residues. The major product was isolated, characterized, and shown to be the triglycosylalditol α-Xyl-(1→3)-α-Fuc-(1→4)-β-Rha-(1→31)-apiitol. This tetrasaccharide fragment of RG-II has three residues in common with a previously characterized heptasaccharide that had been derived from RG-II by partial hydrolysis with acid. RG-II was found to contain a large number of branched galactosyluronic acid residues that have not yet been identified as components of oligosaccharide fragments, although they are undoubtedly part of an octa(galactosyluronic acid) fragment generated by partial acid hydrolysis. The results of sequential partial acid hydrolysis provided evidence that, in RG-II, the extremely acid-labile 3-deoxy-d-manno-2-octulosonic-acid and 3-deoxy-d-lyxo-2-heptulosaric acid residues are attached to O-3 of 3,4-linked galactosyluronic acid residues, and that the mildly acid-labile apiofuranosyl residues are attached to O-2 of 2,4-linked galactosyluronic acid residues. These and previously published data suggested that RG-II has a highly branched structure, arranged around an α-(1→4)-linked galactosyluronic acid backbone.

  Publication DOI: 10.1016/0008-6215(88)84004-7
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Complex Carbohydrate Research Center and Department of Biochemistry, University of Georgia, Russell Research Center of the United States Department of Agriculture, Athens, Georgia, U.S.A.
  Methods: 1H NMR, gel filtration, FAB-MS, partial acid hydrolysis, GC-MS, acid hydrolysis
  
   
  
  Acer pseudoplatanus
  CSDB ID 215517 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: xyloglucan
Contained glycoepitopes: IEDB_114701,IEDB_142488,IEDB_146664,IEDB_983931,SB_192

• Article ID: 10629
  Acebes JL, Moral R, Zarra I "Purification and structure of xyloglucan in pine hypocotyls" - Phytochemistry 33 (1993) 1343-1345
  

  Xyloglucan was purified from water-soluble hemicelluloses extracted with 24% KOH from pine cell walls using ion-exchange chromatography and iodine precipitation. Linkage analysis showed that pine xyloglucan was highly substituted with 80% of the glucosyl residues substituted at position 6. The presence of terminal-fucosyl residues in pine xyloglucan confirm that the primary cell walls of gymnosperms are more closely related to those of dicots than to graminaceous monocot cell walls.

  NCBI PubMed ID: 7763946
  Journal NLM ID: 0151434
  Publisher: Elsevier
  Institutions: Lab. Fisiología Vegetal, Fac. Biología, Universidad de León, León, Spain
  
   
  
  Pinus pinaster
  CSDB ID 146002 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: Gn2M3FX
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_146665,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167186,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86

• Article ID: 11237
  Kajiura H, Seki T, Fujiyama K "Arabidopsis thaliana ALG3 mutant synthesizes immature oligosaccharides in the ER and accumulates unique N-glycans" - Glycobiology 20 (2010) 736-751
  

  The core oligosaccharide Glc3Man9GlcNAc2 is assembled by a series of membrane-bound glycosyltransferases as the lipid carrier dolichylpyrophosphate-linked glycan in the endoplasmic reticulum (ER). The first step of this assembly pathway on the ER luminal side is mediated by ALG3 (asparagine-linked glycosylation 3), which is a highly conserved reaction among eukaryotic cells. Complementary genetics compared with Saccharomyces cerevisiae ALG gene families and bioinformatic approaches have enabled the identification of ALG3 from other species. In Arabidopsis thaliana, AtALG3 (At2g47760) was identified as α1,3-mannosyltransferase. Complementation analysis showed that AtALG3 rescued the temperature-sensitive phenotype, that lipid-linked oligosaccharide assemblies and that protein underglycosylation of S. cerevisiae ALG3-deficient mutant. In Arabidopsis ALG3 mutant, an immature lipid-linked oligosaccharide structure, M5ER, was synthesized, and used for protein N-glycosylation, resulting in the blockade of subsequent maturation with the concanavalin A affinoactive and Endo H-insensitive structure. N-Glycan profiling of total proteins from alg3 mutants exhibited a unique structural profile, alg3 has rare N-glycan structures including Man3GlcNAc2, M4ER, M5ER and GlcM5ER, which are not usually detected in Arabidopsis, and a much less amount of complex-type N-glycan than that in wild type. Interestingly, despite protein N-glycosylation differences compared with wild type, alg3 showed no obvious phenotype under normal and high temperature or salt/osmotic stress conditions. These results indicate that AtALG3 is a critical factor for mature N-glycosylation of proteins, but not essential for cell viability and growth in Arabidopsis.

  Arabidopsis thaliana, N-glycosylation, endoplasmic reticulum, α1, lipid-linked oligosaccharide, 3-mannosyltransferase

  Publication DOI: 10.1093/glycob/cwq028
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: fujiyama@icb.osaka-u.ac.jp
  Institutions: The International Center for Biotechnology, Osaka University, 2-1 Yamada-oka, Suita-shi, Osaka 565, Japan
  Methods: biological assays, HPLC, RP-HPLC, LC-MS/MS, confocal microscopy, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 60972 (all data & tools)
• Article ID: 11238
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 60988 (all data & tools)
• Article ID: 11242
  Kajiura H, Okamoto T, Misaki R, Matsuura Y, Fujiyama K "Arabidopsis β1,2-xylosyltransferase: substrate specificity and participation in the plant-specific N-glycosylation pathway" - Journal of Bioscience and Bioengineering 113 (2012) 48-54
  

  β1,2-Xylosyltransferase (XYLT) is a plant-specific glycosyltransferase that contributes to the biosynthesis of N-glycoproteins in plants. However, the specificity of XYLT for N-glycans has not yet been completely clarified. To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. Recombinant AtXYLT expressed in insect cells required the β1,2-linked N-acetylglucosamine (GlcNAc) residue at the nonreducing terminus of the α1,3-branched mannose (Man) residue (GlcNAcβ1,2-Manα1,3-Man; GNM3B) for activity. However, AtXYLT showed decreased activity with substrates that contained α1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the α1,6-branched Man residue of GlcNAcβ1,2-Man (GlcNAcβ1,2-Manα1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. Moreover, AtXYLT did not show any activity in the transfer of the Xyl residue to N-glycans that contained a mammalian-type β1,4-linked galactose (Gal) residue at the nonreducing terminus of GlcNAcβ1,2-Man. These results indicate that a β1,2-linked GlcNAc residue at the nonreducing terminus of an α1,3-branched Man residue is necessary for AtXYLT activity and that mammalian-type β1,4-linked Gal residue(s) on the same branch completely inhibit(s) the activity. Furthermore, N-glycan analysis showed that approximately 30% of the N-glycans carry the Xyl residue in the wild type. These findings suggest that AtXYLT acts on protein-bound N-glycans prior to α1,3-fucosyltransferase and mannosidase II in planta.

  N-glycan, plant N-glycosylation, Arabidopsis β1, 2-xylosyltransferase, β1, 2-xylosylation, baculovirus

  Publication DOI: 10.1016/j.jbiosc.2011.09.011
  Journal NLM ID: 100888800
  Publisher: Osaka, Japan, Amsterdam, The Netherlands: Society for Bioscience and Bioengineering
  Correspondence: fujiyama@icb.osaka-u.ac.jp
  Institutions: International Center for Biotechnology, Osaka University, 2-1 Yamadaoka, Suita-shi, Osaka 565-0871, Japan, Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita-shi, Osaka 565-0871, Japan
  Methods: biological assays, HPLC, LC-MS/MS, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61029 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: Gn2M3X, Gn2M3
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85

• Article ID: 11237
  Kajiura H, Seki T, Fujiyama K "Arabidopsis thaliana ALG3 mutant synthesizes immature oligosaccharides in the ER and accumulates unique N-glycans" - Glycobiology 20 (2010) 736-751
  

  The core oligosaccharide Glc3Man9GlcNAc2 is assembled by a series of membrane-bound glycosyltransferases as the lipid carrier dolichylpyrophosphate-linked glycan in the endoplasmic reticulum (ER). The first step of this assembly pathway on the ER luminal side is mediated by ALG3 (asparagine-linked glycosylation 3), which is a highly conserved reaction among eukaryotic cells. Complementary genetics compared with Saccharomyces cerevisiae ALG gene families and bioinformatic approaches have enabled the identification of ALG3 from other species. In Arabidopsis thaliana, AtALG3 (At2g47760) was identified as α1,3-mannosyltransferase. Complementation analysis showed that AtALG3 rescued the temperature-sensitive phenotype, that lipid-linked oligosaccharide assemblies and that protein underglycosylation of S. cerevisiae ALG3-deficient mutant. In Arabidopsis ALG3 mutant, an immature lipid-linked oligosaccharide structure, M5ER, was synthesized, and used for protein N-glycosylation, resulting in the blockade of subsequent maturation with the concanavalin A affinoactive and Endo H-insensitive structure. N-Glycan profiling of total proteins from alg3 mutants exhibited a unique structural profile, alg3 has rare N-glycan structures including Man3GlcNAc2, M4ER, M5ER and GlcM5ER, which are not usually detected in Arabidopsis, and a much less amount of complex-type N-glycan than that in wild type. Interestingly, despite protein N-glycosylation differences compared with wild type, alg3 showed no obvious phenotype under normal and high temperature or salt/osmotic stress conditions. These results indicate that AtALG3 is a critical factor for mature N-glycosylation of proteins, but not essential for cell viability and growth in Arabidopsis.

  Arabidopsis thaliana, N-glycosylation, endoplasmic reticulum, α1, lipid-linked oligosaccharide, 3-mannosyltransferase

  Publication DOI: 10.1093/glycob/cwq028
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: fujiyama@icb.osaka-u.ac.jp
  Institutions: The International Center for Biotechnology, Osaka University, 2-1 Yamada-oka, Suita-shi, Osaka 565, Japan
  Methods: biological assays, HPLC, RP-HPLC, LC-MS/MS, confocal microscopy, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 60973 (all data & tools)
• Article ID: 11238
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 60985 (all data & tools)
• Article ID: 11241
  Bencúr P, Steinkellner H, Svoboda B, Mucha J, Strasser R, Kolarich D, Hann S, Köllensperger G, Glössl J, Altmann F, Mach L "Arabidopsis thaliana β1,2-xylosyltransferase: an unusual glycosyltransferase with the potential to act at multiple stages of the plant N-glycosylation pathway" - Biochemical Journal 388 (2005) 515-525
  

  XylT (β1,2-xylosyltransferase) is a unique Golgi-bound glycosyltransferase that is involved in the biosynthesis of glycoprotein-bound N-glycans in plants. To delineate the catalytic domain of XylT, a series of N-terminal deletion mutants was heterologously expressed in insect cells. Whereas the first 54 residues could be deleted without affecting the catalytic activity of the enzyme, removal of an additional five amino acids led to the formation of an inactive protein. Characterization of the N-glycosylation status of recombinant XylT revealed that all three potential N-glycosylation sites of the protein are occupied by N-linked oligosaccharides. However, an unglycosylated version of the enzyme displayed substantial catalytic activity, demonstrating that N-glycosylation is not essential for proper folding of XylT. In contrast with most other glycosyltransferases, XylT is enzymatically active in the absence of added metal ions. This feature is not due to any metal ion directly associated with the enzyme. The precise acceptor substrate specificity of XylT was assessed with several physiologically relevant compounds and the xylosylated reaction products were subsequently tested as substrates of other Golgi-resident glycosyltransferases. These experiments revealed that the substrate specificity of XylT permits the enzyme to act at multiple stages of the plant N-glycosylation pathway.

  glycosyltransferase, Arabidopsis, Xylosyltransferase, Golgi apparatus, N-glycan biosynthesis, proteolytic processing

  Publication DOI: 10.1042/BJ20042091
  Journal NLM ID: 2984726R
  Publisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
  Correspondence: lukas.mach@boku.ac.at
  Institutions: Department für Angewandte Pflanzenwissenschaften und Pflanzenbiotechnologie, Institut für Angewandte Genetik und Zellbiologie, Universität für Bodenkultur Wien, Muthgasse 18, A-1190 Wien, Austria, Department für Chemie, Universität für Bodenkultur Wien, Muthgasse 18, A-1190 Wien, Austria
  Methods: TLC, biological assays, enzymatic assay, MALDI-TOF-MS, size-exclusion chromatography, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61023 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GnM3X
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85

• Article ID: 11238
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 60979 (all data & tools)
• Article ID: 11242
  Kajiura H, Okamoto T, Misaki R, Matsuura Y, Fujiyama K "Arabidopsis β1,2-xylosyltransferase: substrate specificity and participation in the plant-specific N-glycosylation pathway" - Journal of Bioscience and Bioengineering 113 (2012) 48-54
  

  β1,2-Xylosyltransferase (XYLT) is a plant-specific glycosyltransferase that contributes to the biosynthesis of N-glycoproteins in plants. However, the specificity of XYLT for N-glycans has not yet been completely clarified. To gain insights into the function of XYLT in the plant N-glycosylation pathway, we examined the acceptor substrate specificity of recombinant Arabidopsis XYLT (AtXYLT) using 2-aminopyridine-labeled N-glycans as the substrates and confirmed the N-glycans of Arabidopsis xylt mutant. Recombinant AtXYLT expressed in insect cells required the β1,2-linked N-acetylglucosamine (GlcNAc) residue at the nonreducing terminus of the α1,3-branched mannose (Man) residue (GlcNAcβ1,2-Manα1,3-Man; GNM3B) for activity. However, AtXYLT showed decreased activity with substrates that contained α1,3-fucose at the chitobiose core-GlcNAc or a terminal GlcNAc at the α1,6-branched Man residue of GlcNAcβ1,2-Man (GlcNAcβ1,2-Manα1,6-Man; GNM3A), whose ratios were 10% and 50% of the optimal substrate, GNM3B, respectively. Moreover, AtXYLT did not show any activity in the transfer of the Xyl residue to N-glycans that contained a mammalian-type β1,4-linked galactose (Gal) residue at the nonreducing terminus of GlcNAcβ1,2-Man. These results indicate that a β1,2-linked GlcNAc residue at the nonreducing terminus of an α1,3-branched Man residue is necessary for AtXYLT activity and that mammalian-type β1,4-linked Gal residue(s) on the same branch completely inhibit(s) the activity. Furthermore, N-glycan analysis showed that approximately 30% of the N-glycans carry the Xyl residue in the wild type. These findings suggest that AtXYLT acts on protein-bound N-glycans prior to α1,3-fucosyltransferase and mannosidase II in planta.

  N-glycan, plant N-glycosylation, Arabidopsis β1, 2-xylosyltransferase, β1, 2-xylosylation, baculovirus

  Publication DOI: 10.1016/j.jbiosc.2011.09.011
  Journal NLM ID: 100888800
  Publisher: Osaka, Japan, Amsterdam, The Netherlands: Society for Bioscience and Bioengineering
  Correspondence: fujiyama@icb.osaka-u.ac.jp
  Institutions: International Center for Biotechnology, Osaka University, 2-1 Yamadaoka, Suita-shi, Osaka 565-0871, Japan, Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita-shi, Osaka 565-0871, Japan
  Methods: biological assays, HPLC, LC-MS/MS, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61031 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 11238
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 61001 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 11238
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 61002 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 11238
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 61003 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1065.4 [M+Na]+
Trivial name: M3X
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85

• Article ID: 11240
  Zhang M, Henquet M, Chen Z, Zhang H, Zhang Y, Ren X, Van Der Krol S, Gonneau M, Bosch D, Gong Z "LEW3, encoding a putative α-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana" - Plant Journal: for Cell and Molecular Biology 60 (2009) 983-999
  

  N-linked glycosylation is an essential protein modification that helps protein folding, trafficking and translocation in eukaryotic systems. The initial process for N-linked glycosylation shares a common pathway with assembly of a dolichol-linked core oligosaccharide. Here we characterize a new Arabidopsis thaliana mutant lew3 (leaf wilting 3), which has a defect in an α-1,2-mannosyltransferase, a homolog of ALG11 in yeast, that transfers mannose to the dolichol-linked core oligosaccharide in the last two steps on the cytosolic face of the ER in N-glycan precursor synthesis. LEW3 is localized to the ER membrane and expressed throughout the plant. Mutation of LEW3 caused low-level accumulation of Man3GlcNAc2 and Man4GlcNAc2 glycans, structures that are seldom detected in wild-type plants. In addition, the lew3 mutant has low levels of normal high-mannose-type glycans, but increased levels of complex-type glycans. The lew3 mutant showed abnormal developmental phenotypes, reduced fertility, impaired cellulose synthesis, abnormal primary cell walls, and xylem collapse due to disturbance of the secondary cell walls. lew3 mutants were more sensitive to osmotic stress and abscisic acid (ABA) treatment. Protein N-glycosylation was reduced and the unfolded protein response was more activated by osmotic stress and ABA treatment in the lew3 mutant than in the wild-type. These results demonstrate that protein N-glycosylation plays crucial roles in plant development and the response to abiotic stresses.

  α-1, 2-mannosyltransferase, protein N-glycosylation, unfolded protein response, abiotic stresses

  Publication DOI: 10.1111/j.1365-313X.2009.04013.x
  Journal NLM ID: 9207397
  Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
  Correspondence: gongzz@cau.edu.cn
  Institutions: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing, 100193, China, Business Unit Bioscience, Plant Research International, Wageningen University and Research Centre, 6708 PB Wageningen, The Netherlands, Laboratory of Plant Physiology, Wageningen University, The Netherlands, Laboratoire de Biologie Cellulaire, Unité de Recherche 501, Institut Jean-Pierre Bourgin-Institut National de la Recherche Agronomique, Route de St Cyr, 78026 Versailles Cedex, France, Membrane Enzymology, Department of Chemistry, Utrecht University, 3584 CH Utrecht, The Netherlands, China Agricultural University/University of California Riverside Center for Biological Sciences and Biotechnology, National Center for Plant Gene Research, Beijing, China
  Methods: biological assays, microscopy, MALDI-TOF-MS, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61005 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1211.4 [M+Na]+
Trivial name: M3FX
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86

• Article ID: 11240
  Zhang M, Henquet M, Chen Z, Zhang H, Zhang Y, Ren X, Van Der Krol S, Gonneau M, Bosch D, Gong Z "LEW3, encoding a putative α-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana" - Plant Journal: for Cell and Molecular Biology 60 (2009) 983-999
  

  N-linked glycosylation is an essential protein modification that helps protein folding, trafficking and translocation in eukaryotic systems. The initial process for N-linked glycosylation shares a common pathway with assembly of a dolichol-linked core oligosaccharide. Here we characterize a new Arabidopsis thaliana mutant lew3 (leaf wilting 3), which has a defect in an α-1,2-mannosyltransferase, a homolog of ALG11 in yeast, that transfers mannose to the dolichol-linked core oligosaccharide in the last two steps on the cytosolic face of the ER in N-glycan precursor synthesis. LEW3 is localized to the ER membrane and expressed throughout the plant. Mutation of LEW3 caused low-level accumulation of Man3GlcNAc2 and Man4GlcNAc2 glycans, structures that are seldom detected in wild-type plants. In addition, the lew3 mutant has low levels of normal high-mannose-type glycans, but increased levels of complex-type glycans. The lew3 mutant showed abnormal developmental phenotypes, reduced fertility, impaired cellulose synthesis, abnormal primary cell walls, and xylem collapse due to disturbance of the secondary cell walls. lew3 mutants were more sensitive to osmotic stress and abscisic acid (ABA) treatment. Protein N-glycosylation was reduced and the unfolded protein response was more activated by osmotic stress and ABA treatment in the lew3 mutant than in the wild-type. These results demonstrate that protein N-glycosylation plays crucial roles in plant development and the response to abiotic stresses.

  α-1, 2-mannosyltransferase, protein N-glycosylation, unfolded protein response, abiotic stresses

  Publication DOI: 10.1111/j.1365-313X.2009.04013.x
  Journal NLM ID: 9207397
  Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
  Correspondence: gongzz@cau.edu.cn
  Institutions: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing, 100193, China, Business Unit Bioscience, Plant Research International, Wageningen University and Research Centre, 6708 PB Wageningen, The Netherlands, Laboratory of Plant Physiology, Wageningen University, The Netherlands, Laboratoire de Biologie Cellulaire, Unité de Recherche 501, Institut Jean-Pierre Bourgin-Institut National de la Recherche Agronomique, Route de St Cyr, 78026 Versailles Cedex, France, Membrane Enzymology, Department of Chemistry, Utrecht University, 3584 CH Utrecht, The Netherlands, China Agricultural University/University of California Riverside Center for Biological Sciences and Biotechnology, National Center for Plant Gene Research, Beijing, China
  Methods: biological assays, microscopy, MALDI-TOF-MS, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61006 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1268.5 [M+Na]+
Trivial name: GnM3X
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85

• Article ID: 11240
  Zhang M, Henquet M, Chen Z, Zhang H, Zhang Y, Ren X, Van Der Krol S, Gonneau M, Bosch D, Gong Z "LEW3, encoding a putative α-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana" - Plant Journal: for Cell and Molecular Biology 60 (2009) 983-999
  

  N-linked glycosylation is an essential protein modification that helps protein folding, trafficking and translocation in eukaryotic systems. The initial process for N-linked glycosylation shares a common pathway with assembly of a dolichol-linked core oligosaccharide. Here we characterize a new Arabidopsis thaliana mutant lew3 (leaf wilting 3), which has a defect in an α-1,2-mannosyltransferase, a homolog of ALG11 in yeast, that transfers mannose to the dolichol-linked core oligosaccharide in the last two steps on the cytosolic face of the ER in N-glycan precursor synthesis. LEW3 is localized to the ER membrane and expressed throughout the plant. Mutation of LEW3 caused low-level accumulation of Man3GlcNAc2 and Man4GlcNAc2 glycans, structures that are seldom detected in wild-type plants. In addition, the lew3 mutant has low levels of normal high-mannose-type glycans, but increased levels of complex-type glycans. The lew3 mutant showed abnormal developmental phenotypes, reduced fertility, impaired cellulose synthesis, abnormal primary cell walls, and xylem collapse due to disturbance of the secondary cell walls. lew3 mutants were more sensitive to osmotic stress and abscisic acid (ABA) treatment. Protein N-glycosylation was reduced and the unfolded protein response was more activated by osmotic stress and ABA treatment in the lew3 mutant than in the wild-type. These results demonstrate that protein N-glycosylation plays crucial roles in plant development and the response to abiotic stresses.

  α-1, 2-mannosyltransferase, protein N-glycosylation, unfolded protein response, abiotic stresses

  Publication DOI: 10.1111/j.1365-313X.2009.04013.x
  Journal NLM ID: 9207397
  Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
  Correspondence: gongzz@cau.edu.cn
  Institutions: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing, 100193, China, Business Unit Bioscience, Plant Research International, Wageningen University and Research Centre, 6708 PB Wageningen, The Netherlands, Laboratory of Plant Physiology, Wageningen University, The Netherlands, Laboratoire de Biologie Cellulaire, Unité de Recherche 501, Institut Jean-Pierre Bourgin-Institut National de la Recherche Agronomique, Route de St Cyr, 78026 Versailles Cedex, France, Membrane Enzymology, Department of Chemistry, Utrecht University, 3584 CH Utrecht, The Netherlands, China Agricultural University/University of California Riverside Center for Biological Sciences and Biotechnology, National Center for Plant Gene Research, Beijing, China
  Methods: biological assays, microscopy, MALDI-TOF-MS, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61007 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1414.5 [M+Na]+
Trivial name: GnM3FX
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86

• Article ID: 11240
  Zhang M, Henquet M, Chen Z, Zhang H, Zhang Y, Ren X, Van Der Krol S, Gonneau M, Bosch D, Gong Z "LEW3, encoding a putative α-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana" - Plant Journal: for Cell and Molecular Biology 60 (2009) 983-999
  

  N-linked glycosylation is an essential protein modification that helps protein folding, trafficking and translocation in eukaryotic systems. The initial process for N-linked glycosylation shares a common pathway with assembly of a dolichol-linked core oligosaccharide. Here we characterize a new Arabidopsis thaliana mutant lew3 (leaf wilting 3), which has a defect in an α-1,2-mannosyltransferase, a homolog of ALG11 in yeast, that transfers mannose to the dolichol-linked core oligosaccharide in the last two steps on the cytosolic face of the ER in N-glycan precursor synthesis. LEW3 is localized to the ER membrane and expressed throughout the plant. Mutation of LEW3 caused low-level accumulation of Man3GlcNAc2 and Man4GlcNAc2 glycans, structures that are seldom detected in wild-type plants. In addition, the lew3 mutant has low levels of normal high-mannose-type glycans, but increased levels of complex-type glycans. The lew3 mutant showed abnormal developmental phenotypes, reduced fertility, impaired cellulose synthesis, abnormal primary cell walls, and xylem collapse due to disturbance of the secondary cell walls. lew3 mutants were more sensitive to osmotic stress and abscisic acid (ABA) treatment. Protein N-glycosylation was reduced and the unfolded protein response was more activated by osmotic stress and ABA treatment in the lew3 mutant than in the wild-type. These results demonstrate that protein N-glycosylation plays crucial roles in plant development and the response to abiotic stresses.

  α-1, 2-mannosyltransferase, protein N-glycosylation, unfolded protein response, abiotic stresses

  Publication DOI: 10.1111/j.1365-313X.2009.04013.x
  Journal NLM ID: 9207397
  Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
  Correspondence: gongzz@cau.edu.cn
  Institutions: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing, 100193, China, Business Unit Bioscience, Plant Research International, Wageningen University and Research Centre, 6708 PB Wageningen, The Netherlands, Laboratory of Plant Physiology, Wageningen University, The Netherlands, Laboratoire de Biologie Cellulaire, Unité de Recherche 501, Institut Jean-Pierre Bourgin-Institut National de la Recherche Agronomique, Route de St Cyr, 78026 Versailles Cedex, France, Membrane Enzymology, Department of Chemistry, Utrecht University, 3584 CH Utrecht, The Netherlands, China Agricultural University/University of California Riverside Center for Biological Sciences and Biotechnology, National Center for Plant Gene Research, Beijing, China
  Methods: biological assays, microscopy, MALDI-TOF-MS, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61008 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1471.6 [M+Na]+
Trivial name: Gn2M3X
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_167188,IEDB_167189,IEDB_174332,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85

• Article ID: 11240
  Zhang M, Henquet M, Chen Z, Zhang H, Zhang Y, Ren X, Van Der Krol S, Gonneau M, Bosch D, Gong Z "LEW3, encoding a putative α-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana" - Plant Journal: for Cell and Molecular Biology 60 (2009) 983-999
  

  N-linked glycosylation is an essential protein modification that helps protein folding, trafficking and translocation in eukaryotic systems. The initial process for N-linked glycosylation shares a common pathway with assembly of a dolichol-linked core oligosaccharide. Here we characterize a new Arabidopsis thaliana mutant lew3 (leaf wilting 3), which has a defect in an α-1,2-mannosyltransferase, a homolog of ALG11 in yeast, that transfers mannose to the dolichol-linked core oligosaccharide in the last two steps on the cytosolic face of the ER in N-glycan precursor synthesis. LEW3 is localized to the ER membrane and expressed throughout the plant. Mutation of LEW3 caused low-level accumulation of Man3GlcNAc2 and Man4GlcNAc2 glycans, structures that are seldom detected in wild-type plants. In addition, the lew3 mutant has low levels of normal high-mannose-type glycans, but increased levels of complex-type glycans. The lew3 mutant showed abnormal developmental phenotypes, reduced fertility, impaired cellulose synthesis, abnormal primary cell walls, and xylem collapse due to disturbance of the secondary cell walls. lew3 mutants were more sensitive to osmotic stress and abscisic acid (ABA) treatment. Protein N-glycosylation was reduced and the unfolded protein response was more activated by osmotic stress and ABA treatment in the lew3 mutant than in the wild-type. These results demonstrate that protein N-glycosylation plays crucial roles in plant development and the response to abiotic stresses.

  α-1, 2-mannosyltransferase, protein N-glycosylation, unfolded protein response, abiotic stresses

  Publication DOI: 10.1111/j.1365-313X.2009.04013.x
  Journal NLM ID: 9207397
  Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
  Correspondence: gongzz@cau.edu.cn
  Institutions: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing, 100193, China, Business Unit Bioscience, Plant Research International, Wageningen University and Research Centre, 6708 PB Wageningen, The Netherlands, Laboratory of Plant Physiology, Wageningen University, The Netherlands, Laboratoire de Biologie Cellulaire, Unité de Recherche 501, Institut Jean-Pierre Bourgin-Institut National de la Recherche Agronomique, Route de St Cyr, 78026 Versailles Cedex, France, Membrane Enzymology, Department of Chemistry, Utrecht University, 3584 CH Utrecht, The Netherlands, China Agricultural University/University of California Riverside Center for Biological Sciences and Biotechnology, National Center for Plant Gene Research, Beijing, China
  Methods: biological assays, microscopy, MALDI-TOF-MS, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61009 (all data & tools)