| Literature DB >> 10872230 |
W Zhang1, W J Peumans, A Barre, C H Astoul, P Rovira, P Rougé, P Proost, P Truffa-Bachi, A A Jalali, E J Van Damme.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2000 PMID: 10872230 DOI: 10.1007/s004250050705
Source DB: PubMed Journal: Planta ISSN: 0032-0935 Impact factor: 4.116