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Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plants |
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| Authors: | Wenling Zhang Willy J Peumans Annick Barre Corinne Houles Astoul Paula Rovira Pierre Rougé Paul Proost Paolo Truffa-Bachi Ali A H Jalali Els J M Van Damme |
| Institution: | (1) Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem de Croylaan 42, 3001 Leuven, Belgium, BE;(2) Institut de Pharmacologie et Biologie Structurale, UPR CNRS 9062, 205 Route de Narbonne, 31077 Toulouse Cedex, France, FR;(3) Unité d'Immunophysiologie Moléculaire, CNRS LA 1961, Département d'Immunologie, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris Cedex 15, France, FR;(4) Rega Institute, Laboratory of Molecular Immunology, Katholieke Universiteit Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium, BE |
| Abstract: | A novel plant lectin was isolated from salt-stressed rice (Oryzasativa 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. Received: 27 July 1999 / Accepted: 11 November 1999 |
| Keywords: | : Jacalin – Lectin – Oryza (salt stress) – Salt stress – Stress protein |
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