Glycosylation of the cationic peanut peroxidase gene expressed in transgenic tobacco

被引：4

作者：

Bao, LG

Ma, SW

van Huystee, RB ^{[1
]}

机构：

[1] Univ Western Ontario, Dept Plant Sci, London, ON N6A 5B7, Canada

[2] Siebens Drake Res Inst, London, ON N6G 2V4, Canada

来源：

PLANT SCIENCE | 2000年 / 156卷 / 01期

基金：

加拿大自然科学与工程研究理事会;

关键词：

peroxidase; peanut; N-linked glycans; monosaccharide; glycosylation; transgenic tobacco;

D O I：

10.1016/S0168-9452(00)00233-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The major cationic peanut (Arachis hypogaea) peroxidase, secreted into the extracellular space, is a glycoprotein with three N-linked glycans (polysaccharides) which are connected to the peptide backbone at Asn-60, Asn-144 and Asn-185. In this report, a C-terminal histidine-tagged cationic peanut peroxidase gene was expressed in transgenic tobacco (Nicotiana tabacum). Tissue of the transgenic tobacco was cultured in suspension culture and the his-tagged peroxidase was purified in large quantities from 14-day-old suspension culture. The number of glycans, glycosylation sites and the chemical nature of glycan moieties attached to cationic peanut peroxidase expressed in transgenic tobacco were examined. Cationic peanut peroxidase isolated From the above transgenic tobacco had the identical number of complex glycans, attached at the same glycosylation sites as on cationic peanut peroxidase isolated from peanut suspension culture. Monosaccharide components of these glycans are N-acetylglucosamine (GlcNAc), mannose (Man), fucose (Fuc), xylose (Xyl) and galactose (Gal), the same sugars as found in native cationic peanut peroxidase. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：55 / 63

页数：9

共 36 条

[1] THE BETA-1-]2-D-XYLOSE AND ALPHA-1-]3-L-FUCOSE SUBSTITUTED N-LINKED OLIGOSACCHARIDES FROM ERYTHRINA-CRISTAGALLI LECTIN - ISOLATION, CHARACTERIZATION AND COMPARISON WITH OTHER LEGUME LECTINS [J].