Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plants

被引：0
|
作者：
Zhang, WL
Peumans, WJ
Barre, A
Astoul, CH
Rovira, P
Rougé, P
Proost, P
Truffa-Bachi, P
Jalali, AAH
Van Damme, EJM
机构：
[1] Katholieke Univ Leuven, Lab Phytopathol & Plant Protect, B-3001 Louvain, Belgium
[2] CNRS, Inst Pharmacol & Biol Struct, UPR 9062, F-31077 Toulouse, France
[3] Inst Pasteur, Unite Immunophysiol Mol, CNRS, LA 1961,Dept Immunol, F-75724 Paris 15, France
[4] Katholieke Univ Leuven, Rega Inst, Lab Mol Immunol, B-3000 Louvain, Belgium
来源：
PLANTA | 2000年 / 210卷 / 06期
关键词：
jacalin; lectin; Oryza (salt stress); salt stress; stress protein;
D O I：
暂无
中图分类号：
Q94 [植物学];
学科分类号：
071001 ;
摘要：
A novel plant lectin was isolated from salt-stressed rice (Oryza sativa L.) plants and partially characterized. The lectin occurs as a natural mixture of two closely related isoforms consisting of two identical non-covalently linked subunits of 15 kDa. Both isoforms are best inhibited by mannose and exhibit potent mitogenic activity towards T-lymphocytes. Biochemical analyses and sequence comparisons further revealed that the rice lectins belong to the subgroup of mannose-binding jacalin-related lectins. In addition, it could be demonstrated that the lectins described here correspond to the protein products of previously described salt-stress-induced genes. Our results not only identify the rice lectin as a stress protein but also highlight the possible importance of protein-carbohydrate interactions in stress responses in plants.
引用
收藏
页码：970 / 978
页数：9
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