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Journal of Biochemistry Advance Access published online on December 13, 2006
Journal of Biochemistry, doi:10.1093/jb/mvm021
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© 2006 The Japanese Biochemical Society

Site-specific glycosylation at Asn-292 in ovalbumin is essential to efficient secretion in yeast

Kazunari Ito, Akiko Seri, Fukiko Kimura and Naotoshi Matsudomi*

Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515, Japan

*To whom correspondence should be addressed. Tel: +81-83-933-5853; Fax: +81-83-933-5820; E-mail: naotoshi{at}yamaguchi-u.ac.jp

Received November 9, 2006; Accepted November 28, 2006


  Abstract

Chicken ovalbumin (OVA) exists as mono–N–glycosylated form with a carbohydrate chain on Asn–292 in egg white, despite the possession of two potential N–glycosylation sites. To investigate the roles of N–glycosylation of OVA, we constructed a series of N–glycosylation mutants deleted N–glycosylation site and compared the secretion level of the mutants in Pichia pastoris. N292Q and N292/311Q mutants resulted in greater lowering of the secretion level as compared to wild–type, whereas N311Q mutant was secreted in approximately equal amounts to wild–type. However, secretion of wild–type and N311Q mutant was inhibited completely by tunicamycin treatment. All the N–glycosylation mutants have been expressed in the cells, as well as wild–type. CD and fluorescence spectra of secreted N311Q mutant were almost identical to those of wild–type, while those of N292Q and N292/311Q mutants were different from wild–type. And, N292Q and N292/311Q mutants showed considerably lower denaturation temperature than wild–type. The results indicate that N–glycosylation at Asn–292 of OVA is required for the folding and secretion.

Key Words: ovalbumin, N–glycosylation, folding, secretion, Pichia pastoris


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