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Gewählte Publikation:

Publikationstyp: Zeitschriftenaufsatz
Dokumentart: Originalarbeit

Publikationsjahr: 2013

AutorInnen: Yan, S; Serna, S; Reichardt, NC; Paschinger, K; Wilson, IB

Titel: Array-assisted characterization of a fucosyltransferase required for the biosynthesis of complex core modifications of nematode N-glycans.

Quelle: J Biol Chem. 2013; 288(29):21015-21028



Autor/innen der Vetmeduni Vienna:

Yan Shi

Diese Publikation wurde nicht im Namen der Vetmeduni Vienna erstellt und ist deshalb ausschließlich der persönlichen Publikationsliste des/der Autors/Autorin zugeordnet!


Abstract:
Fucose is a common monosaccharide component of cell surfaces and is involved in many biological recognition events. Therefore, definition and exploitation of the specificity of the enzymes (fucosyltransferases) involved in fucosylation is a recurrent theme in modern glycosciences. Despite various studies, the specificities of many fucosyltransferases are still unknown, so new approaches are required to study these. The model nematode Caenorhabditis elegans expresses a wide range of fucosylated glycans, including N-linked oligosaccharides with unusual complex core modifications. Up to three fucose residues can be present on the standard N,N"-diacetylchitobiose unit of these N-glycans, but only the fucosyltransferases responsible for transfer of two of these (the core α1,3-fucosyltransferase FUT-1 and the core α1,6-fucosyltransferase FUT-8) were previously characterized. By use of a glycan library in both array and solution formats, we were able to reveal that FUT-6, another C. elegans α1,3-fucosyltransferase, modifies nematode glycan cores, specifically the distal N-acetylglucosamine residue; this result is in accordance with glycomic analysis of fut-6 mutant worms. This core-modifying activity of FUT-6 in vitro and in vivo is in addition to its previously determined ability to synthesize Lewis X epitopes in vitro. A larger scale synthesis of a nematode N-glycan core in vitro using all three fucosyltransferases was performed, and the nature of the glycosidic linkages was determined by NMR. FUT-6 is probably the first eukaryotic glycosyltransferase whose specificity has been redefined with the aid of glycan microarrays and so is a paradigm for the study of other unusual glycosidic linkages in model and parasitic organisms.

Keywords Pubmed: Animals
Biosynthetic Pathways
Caenorhabditis elegans/enzymology*
Caenorhabditis elegans Proteins/metabolism*
Fucose/chemistry
Fucose/metabolism
Fucosyltransferases/metabolism*
Glycomics
Glycosylation
Magnetic Resonance Spectroscopy
Mass Spectrometry
Microarray Analysis*
Mutant Proteins/metabolism
Polysaccharides/biosynthesis*
Polysaccharides/chemistry
Polysaccharides/metabolism
Solutions
Substrate Specificity


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