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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-05

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

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. More... »

PAGES

970-978

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s004250050705

DOI

http://dx.doi.org/10.1007/s004250050705

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029000317

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10872230


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