Review/N-glycans: The making of a varied toolbox

Lannoo, Nausicaä; Damme, Els J.M. Van

doi:10.1016/j.plantsci.2015.06.023

Cited by 73 publications

(57 citation statements)

References 156 publications

(151 reference statements)

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“…Eukaryotic cells also have Dol-P-hexose that serves as the monosaccharide donor for the addition of terminal mannose and glucose residues to complete the synthesis of the 14-residue N-glycan structure on the lumenal face of the endoplasmic reticulum membranes (8). In Eubacteria, E. coli, and Shigella flexneri, Pren-P-hexose also coexists with the polyprenoldiphosphate type LLO.…”

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Taguchi

Fujinami

Kohda

2016

Journal of Biological Chemistry

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The glycosylation of asparagine residues is the predominant protein modification in all three domains of life. An oligosaccharide chain is preassembled on a lipid-phospho carrier and transferred onto asparagine residues by the action of a membrane-bound enzyme, oligosaccharyltransferase. The oligosaccharide donor for the oligosaccharyl transfer reaction is dolichol-diphosphate-oligosaccharide in Eukaryota and polyprenol-diphosphate-oligosaccharide in Eubacteria. The donor in some archaeal species was reportedly dolichol-monophosphate-oligosaccharide. Thus, the difference in the number of phosphate groups aroused interest in whether the use of the dolichol-monophosphate type donors is widespread in the domain Archaea. Currently, all of the archaeal species with identified oligosaccharide donors have belonged to the phylum Euryarchaeota. Here, we analyzed the donor structures of two species belonging to the phylum Crenarchaeota, Pyrobaculum calidifontis and Sulfolobus solfataricus, in addition to two species from the Euryarchaeota, Pyrococcus furiosus and Archaeoglobus fulgidus. The electrospray ionization tandem mass spectrometry analyses confirmed that the two euryarchaeal oligosaccharide donors were the dolichol-monophosphate type and newly revealed that the two crenarchaeal oligosaccharide donors were the dolichol-diphosphate type. This novel finding is consistent with the hypothesis that the ancestor of Eukaryota is rooted within the TACK (Thaum-, Aig-, Cren-, and Korarchaeota) superphylum, which includes Crenarchaea. Our comprehensive study also revealed that one archaeal species could contain two distinct oligosaccharide donors for the oligosaccharyl transfer reaction. The A. fulgidus cells contained two oligosaccharide donors bearing oligosaccharide moieties with different backbone structures, and the S. solfataricus cells contained two oligosaccharide donors bearing stereochemically different dolichol chains.The glycosylation of asparagine residues is the predominant protein modification throughout all three domains of life (1-3). The oligosaccharides attached to asparagine residues in glycoproteins (N-glycan) affect various properties of the proteins, including folding, conformation, solubility, and antigenicity. Carbohydrate-binding proteins, such as lectins, recognize the N-glycans. Within the lumen of the endoplasmic reticulum in eukaryotic cells, the N-glycan functions as a quality control tag in the endoplasmic reticulum-associated degradation (4). The N-glycosylation occurs in the consensus motif (referred to as the sequon) represented by Asn-Xaa-Ser/Thr, where Xaa can be any residue except Pro. The formation of the N-glycosidic bond, between the monosaccharide residue at the reducing end of an oligosaccharide and the side chain amide group of the asparagine residues in proteins, is catalyzed by a membranebound enzyme, oligosaccharyltransferase (OST) 2 (3). The eukaryotic OST enzyme is a multisubunit protein complex. Among the eight different membrane subunit proteins, the catalytic subunit is a po...

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Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Taguchi

Fujinami

Kohda

2016

Journal of Biological Chemistry

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“…However, little is known about the structure-to-function relationship of N-glycan during plant growth. It is understood that ER-localized enzymes are more critical than Golgi-localized enzymes in morphological abnormalities of plants [5], and that N-glycan biosynthetic downstream glycosyltransferase, b1,2-xylosyltransferase, and a1,3-fucosyltransferase are associated with salt and osmotic stress tolerance in plants [6].…”

Section: Introductionmentioning

confidence: 99%

N-glycan transition of the early developmental stage in Oryza sativa

Horiuchi

Hirotsu

Miyanishi

2016

Biochemical and Biophysical Research Communications

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“…Biological activities of many therapeutic proteins rely heavily on their glycosylation status. As a result, protein glycosylation is one of the main focuses in the biopharmaceutical research community1012. Carbohydrates attached to the proteins can be classified into two categories, N -glycans, which are linked to the amide group of asparagine residues, and O -glycans, present on the hydroxyl group of serine, threonine, hydroxylysine and hydroxyproline residues10.…”

mentioning

confidence: 99%

“…The mechanisms are initialized at the cytosolic side of the ER membrane by transferring an oligosaccharide precursor, Man 5 GlcNAc 2 , from a dolichol lipid carrier onto specific Asn residues constitutive of the consensus sequence Asn-X-Ser/Thr/Cys in nascent proteins10131415. Afterward, reactions proceed in ER lumen with complete assembly of the Glc 3 Man 9 GlcNAc 2 precursor catalyzed by sequential orchestration of multiple enzymatic steps101216.…”

mentioning

confidence: 99%

Evolution of protein N-glycosylation process in Golgi apparatus which shapes diversity of protein N-glycan structures in plants, animals and fungi

Wang

Gai

et al. 2017

Sci Rep

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Protein N-glycosylation (PNG) is crucial for protein folding and enzymatic activities, and has remarkable diversity among eukaryotic species. Little is known of how unique PNG mechanisms arose and evolved in eukaryotes. Here we demonstrate a picture of onset and evolution of PNG components in Golgi apparatus that shaped diversity of eukaryotic protein N-glycan structures, with an emphasis on roles that domain emergence and combination played on PNG evolution. 23 domains were identified from 24 known PNG genes, most of which could be classified into a single clan, indicating a single evolutionary source for the majority of the genes. From 153 species, 4491 sequences containing the domains were retrieved, based on which we analyzed distribution of domains among eukaryotic species. Two domains in GnTV are restricted to specific eukaryotic domains, while 10 domains distribute not only in species where certain unique PNG reactions occur and thus genes harboring these domains are supoosed to be present, but in other ehkaryotic lineages. Notably, two domains harbored by β-1,3 galactosyltransferase, an essential enzyme in forming plant-specific Lea structure, were present in separated genes in fungi and animals, suggesting its emergence as a result of domain shuffling.

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Review/N-glycans: The making of a varied toolbox

Cited by 73 publications

References 156 publications

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

N-glycan transition of the early developmental stage in Oryza sativa

Evolution of protein N-glycosylation process in Golgi apparatus which shapes diversity of protein N-glycan structures in plants, animals and fungi

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