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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Chromatography, Ion Exchange
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Electrophoresis, Polyacrylamide Gel
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Hemagglutination Tests
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Humans
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Lectins / chemistry
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Lectins / isolation & purification*
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Lectins / metabolism
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Lectins / pharmacology
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Mannose / metabolism*
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Mannose-Binding Lectins*
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Mass Spectrometry
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Mice
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Mice, Inbred BALB C
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Mice, Inbred C57BL
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Models, Molecular
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Molecular Sequence Data
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Oryza / metabolism*
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Oryza / physiology
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Plant Lectins
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Plant Proteins / chemistry
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Plant Proteins / isolation & purification*
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Plant Proteins / metabolism
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Plant Proteins / pharmacology
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Protein Structure, Tertiary
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Rabbits
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Sequence Alignment
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Sodium Chloride / metabolism*
Substances
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Lectins
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Mannose-Binding Lectins
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Plant Lectins
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Plant Proteins
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jacalin
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orysata protein, Oryza sativa
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Sodium Chloride
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Mannose