Identification and Characterization of an Intracellular Lectin, Calnexin, from Aspergillus oryzae Using N-Glycan-Conjugated Beads
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概要
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Recently, asparagine-linked oligosaccharides (N-glycans) have been found to play a pivotal role in glycoprotein quality control in the endoplasmic reticulum (ER). In order to screen proteins interacting with N-glycans, we developed affinity chromatography by conjugating synthetic N-glycans on sepharose beads. Using the affinity beads with the dodecasaccharide Glc1Man9GlcNAc2, one structure of the N-glycans, a 75-kDa protein, was isolated from the membranous fraction including the ER in Aspergillus oryzae. By LC-MS/MS analysis using the A. oryzae genome database, the protein was identified as one (AO090009000313) sharing similarities with calnexin. Further affinity chromatographic experiments suggested that the protein specifically bound to Glc1Man9GlcNAc2, similarly to mammalian calnexins. We designated the gene AoclxA and expressed it as a fusion gene with egfp, revealing the ER localization of the AoClxA protein. Our results suggest that our affinity chromatography with synthetic N-glycans might help in biological analysis of glycoprotein quality control in the ER.
- 社団法人 日本農芸化学会の論文
著者
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Kitamoto Katsuhiko
Department of Biotechnology, The University of Tokyo
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Ito Yukishige
RIKEN Advanced Science Institute and ERATO Japan Science and Technology Agency, Wako, Saitama 351-01
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MARUYAMA Jun-ichi
Department of Biotechnology, The University of Tokyo
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Maruyama J
Dep. Of Biotechnology Graduate School Of Agricultural And Life Sciences The Univ. Of Tokyo
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Watanabe Taisuke
RIKEN (The Institute of Physical and Chemical Research)
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Matsuo Ichiro
RIKEN (The Institute of Physical and Chemical Research)
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