Taxonomic group: plant / Streptophyta
(Phylum: Streptophyta)
Publication DOI: 10.1074/jbc.M115.653162Journal NLM ID: 2985121RPublisher: 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
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
Structure type: oligomer
Location inside paper: Figure 8
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_140628,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153543,IEDB_153755,IEDB_164174,IEDB_232584,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
Comments, role: presumable pathway of N-glycan processing
Related record ID(s): 60974, 60975, 60976, 60977, 60978, 60979, 60980, 60981, 60982, 60983, 60984, 60985, 60986, 60987, 60988, 60989, 60990, 60991, 60992, 60993, 60994, 60996, 60997, 60998, 60999, 61000, 61001, 61002, 61003
NCBI Taxonomy refs (TaxIDs): 3702
Show glycosyltransferases
There are too many chemically distinct structures (~512), so only one is shown:
?DGlcp(1-2)?DGlcp(1-3)?DGlcp(1-3)aDManp(1-2)aDManp(1-2)aDManp(1-3)[aDManp(1-2)aDManp(1-3)[aDManp(1-2)aDManp(1-6)]aDManp(1-6)]bDManp(1-4)[Ac(1-2)]bDGlcpN(1-4)[Ac(1-2)]bDGlcpN1N(1-4)x?Asn?
Found 
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