Abstract:-The mobilization of seed proteins from Pisum arvense L. during germination in the absence of light was studied. The seeds were found to be completely consumed 22 days after germination and seedlings ceased growth after the 18 th day. SDS-PAGE indicated that the main protein bands correspond to high molecular mass storage proteins which undergo proteolysis in the initial stages of germination and are not detected after the 7 th day of germination. However, the corresponding lectin profiles were detected during… Show more
“…This content increased after four days of germination and then even more when the stage of seedling was reached [12]. There's a possibility that at least a part of the increase in Abu concentration may be explained by the release of this molecule when the canonical dimmer is disrupted, when the lectins start to be consumed during final steps of germination [22]. Consequently free Abu increases in the seedlings.…”
Section: Resultsmentioning
confidence: 99%
“…Once lectins are consumed at the end of germination, it's reasonable to assume that there could be a correlation between lectin-binding substances such as Abu and the development of plant response against stress and pathogens [11,22]. …”
BackgroundLectins are mainly described as simple carbohydrate-binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds (CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA-like lectins; a site where a non-protein amino-acid, α-aminobutyric acid (Abu), is bound.ResultsThe overall structure of native CGL and complexed with α-methyl-mannoside and Abu have been refined at 2.3 Å and 2.31 Å resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry.ConclusionThe presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.
“…This content increased after four days of germination and then even more when the stage of seedling was reached [12]. There's a possibility that at least a part of the increase in Abu concentration may be explained by the release of this molecule when the canonical dimmer is disrupted, when the lectins start to be consumed during final steps of germination [22]. Consequently free Abu increases in the seedlings.…”
Section: Resultsmentioning
confidence: 99%
“…Once lectins are consumed at the end of germination, it's reasonable to assume that there could be a correlation between lectin-binding substances such as Abu and the development of plant response against stress and pathogens [11,22]. …”
BackgroundLectins are mainly described as simple carbohydrate-binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds (CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA-like lectins; a site where a non-protein amino-acid, α-aminobutyric acid (Abu), is bound.ResultsThe overall structure of native CGL and complexed with α-methyl-mannoside and Abu have been refined at 2.3 Å and 2.31 Å resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry.ConclusionThe presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.
“…Ultrastructural and histochemical evidence of proteins could be found in cotyledon cells of mature seeds in C. echinata, which showed numerous free ribosomes, rough endoplasmic reticulum, mitochondriae with developed cristae and strongly Aniline Blue Black-stained contents in cells. According to Silva et al (2000), proteins which were largely stored in sub cellular compartments and were not mobilized during the seed germination could be lecithins, these have been observed in the cotyledons of other species of Leguminosae, mainly Papilionoideae. Lecithins would act as defense proteins against predators and pathogens and would protect cotyledons while mobilization of the storage substances is being carried out (Cavada et al, 1993).…”
“…During germination, protein bodies break down into amino acids for the growing seedling, showing different patterns of protein mobilization. ConBr may have a role as storage protein, while seed lectins in legume plants may play other biological roles (Cavada et al, 1990;Moreira et al, 1993;Silva et al, 2000). This fact may justify the presence of ConBr at the endosperm.…”
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