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Taxonomic group: fungi / Ascomycota (Phylum: Ascomycota)

The structure was elucidated in this paper
NCBI PubMed ID: 21622726
Publication DOI: 10.1093/glycob/cwr073
Journal NLM ID: 9104124
Publisher: IRL Press at Oxford University Press
Correspondence: tsuzuki_gm

riken.jp
Institutions: Glycometabolome Team, Systems Glycobiology Research Group, RIKEN Advanced Science Institute, Wako, Japan

In eukaryotic cells, it is known that N-glycans play a pivotal role in quality control of carrier proteins. Although "free" forms of oligosaccharides (fOSs) are known to be accumulated in the cytosol, the precise mechanism of their formation, degradation and biological relevance remains poorly understood. It has been shown that, in budding yeast, almost all fOSs are formed from misfolded glycoproteins. Precise structural analysis of fOSs revealed that several yeast fOSs bear a yeast-specific modification by Golgi-resident α-1,6-mannosyltransferase, Och1. In this study, structural diversity of fOSs in och1Δ cells was analyzed. To our surprise, several fOSs in och1Δ cells have unusual α-1,3-linked mannose residues at their non-reducing termini. These mannose residues were not observed in wild-type cells, suggesting that the addition of these unique mannoses occurred as a compensation of Och1 defect. A significant increase in the amount of fOSs modified by Golgi-localized mannosyltransferases was also observed in och1Δ cells. Moreover, the amount of processed fOSs and intracellular α-mannosidase (Ams1) both increased in this mutant. Up-regulation of Ams1 activity was also apparent for cells treated with cell wall perturbation reagent. These results provide an insight into a possible link between catabolism of fOSs and cell wall stress.

N-glycan, yeast, free oligosaccharides, α-mannosidase, cell wall stress

Structure type: oligomer ; 1983.0 [M+Na]+
Location inside paper: table III, M9H
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_187238,IEDB_187239,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

Methods: GC, MALDI-TOF MS, HPLC, GPC, enzymatic digestion, extraction, CC, cell growth, pyridylamination, enzymatic assay
Enzymes that release or process the structure: α-1,6-mannosyltransferase (Och1), α-1,2-mannosidase, α-1,2/3-mannosidase
Comments, role: relative amount = 7.5%

Related record ID(s): 43514, 43515, 43516, 43517, 43518, 43519, 43521, 43522, 43523, 43524, 43525, 43526, 43527, 43528, 43529, 43530, 43531, 43532, 43533, 43534, 43535
NCBI Taxonomy refs (TaxIDs): 1247190
Reference(s) to other database(s): GTC:G97455PT
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@@H]1[C@@H](O)[C@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO[C@H]4O[C@H](CO[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H]4O)[C@@H](O)[C@H](O[C@H]4O[C@H](CO[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H]3O)[C@H](O)[C@H]2NC(C)=O)[C@@H](CO)O[C@H]1O

SVG MW SMILES 3D mol Ionize