Arabidopsis β1,2-xylosyltransferase : Substrate specificity and participation in the plant-specific N-glycosylation pathway(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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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.
著者
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Fujiyama Kazuhito
International Center for Biotechnology, Osaka University
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Kazuhito Fujiyama
International Center For Biotechnology Osaka University
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Fujiyama Kazuhito
大阪大学生物工学国際交流センター
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Fujiyama Kazuhito
International Center For Biotechnology Osaka Univ.
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Fujiyama Kazuhito
Department Of Fermentation Technology Osaka University
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Fujiyama Kazuhito
International Center For Biotechnology Osaka University
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Misaki Ryo
International Center For Biotechnology Osaka University
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Misaki Ryo
The International Center For Biotechnology Osaka University
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Matsuura Yoshiharu
Department Of Hygiene And Microbiology Faculty Of Veterinary Medicine Hokkaido University
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Okamoto Toru
Department Of Molecular Virology Research Institute For Microbial Diseases Osaka University
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Fujiyama Kazuhito
The International Center For Biotechnology Osaka Univ. 2-1 Yamada-oka Suita Osaka 565-0871 Jpn
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Kajiura Hiroyuki
International Center For Biotechnology Osaka University
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Okamoto Toru
Department Of Molecular Virology Research Institute For Microbial Diseases Osaka University:(present
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Okamoto Toru
Department of Chemistry, Faculty of Science, Kyushu University 33
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