lectin/oryza sativa

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Interaction of asparagine-linked oligosaccharides with an immobilized rice (Oryza sativa) lectin column.

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The carbohydrate-binding specificity of rice (Oryza sativa) lectin was investigated by testing the ability of radioactively labelled glycopeptides and oligosaccharides to bind to a rice lectin-Sepharose 4B column. Rice lectin binds asparagine-linked oligosaccharides through the core

Lectin Sequence Distribution in QTLs from Rice (Oryza sativa) Suggest A Role in Morphological Traits and Stress Responses.

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Rice (Oryza sativa) is one of the main staple crops worldwide but suffers from important yield losses due to different abiotic and biotic stresses. Analysis of quantitative trait loci (QTL) is a classical genetic method which enables the creation of more resistant cultivars but does not yield

Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs).

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Eicosapenta peptide repeats (EPRs) occur exclusively in flowering plant genomes and exhibit very high amino acid residue conservation across occurrence. DNA and amino acid sequence searches yielded no indications about the function due to absence of similarity to known sequences. Tertiary structure

Cloning and expression of a novel cDNA encoding a mannose-specific jacalin-related lectin from Oryza sativa.

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Lectin plays an important role in defense signaling in plants. A few genes of this family have been cloned. Here we report on a mannose-specific jacalin-related lectin in rice. Using sequence information of wheat gene VER2, which we had previously cloned, we were able to amplify a cDNA of OsJAC1

Interaction of rice (Oryza sativa) lectin with N-acetylglucosaminides. Fluorescence studies.

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The interaction of lectin isolated from rice (Oryza sativa) embryos with N-acetylglucosaminides was studied by equilibrium dialysis and fluorescence. Equilibrium dialysis with 4-methylumbelliferyl-(GlcNac)2 showed that rice lectin (Mr 38000) contains four equivalent saccharide-binding sites.

Purification, crystallization and preliminary X-ray crystallographic analysis of rice lectin from Oryza sativa.

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Lectins with sugar-binding specificity are widely distributed in higher plants and various other species. The expression of rice lectin from Oryza sativa is up-regulated in the growing coleoptile when anaerobic stress persists. A rice lectin of molecular weight 15.2 kDa has been crystallized using

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

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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

Expression and purification of the recombinant SALT lectin from rice (Oryza sativa L.).

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The SALT protein is a 14.5 kDa mannose-binding lectin, originally described as preferentially expressed in rice plant roots in response to NaCl stress. Recombinant SALT lectin was produced in Escherichia coli from a cDNA clone encoding protein. After isopropyl-beta-d-thiogalactopyranoside induction,

Subcellular site of lectin synthesis in developing rice embryos.

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Embryos of developing rice (Oryza sativa L. cv. Koshihikari) caryopses which actively synthesize lectin were labelled with [S]cysteine for different times and newly synthesized rice lectin was isolated by affinity chromatography. Gel filtration of embryo extracts on Sepharose-4B indicated that a

Vinyl sulfone functionalization: a feasible approach for the study of the lectin-carbohydrate interactions.

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Carbohydrate-mediated molecular recognition is involved in many biological aspects such as cellular adhesion, immune response, blood coagulation, inflammation, and infection. Considering the crucial importance of such biological events in which proteins are normally involved, synthetic

Isolation, molecular and biological properties of a lectin from rice embryo: relationship with wheat germ agglutinin properties.

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Rice lectin (Oryza sativa, var. Balilla 28) was purified from defatted embryos by aqueous acid extraction at pH 1.3 followed by ammonium sulfate precipitation between 2 and 4 M, affinity chromatography on agarose-p-aminophenyl-beta-D-N-acetylglucosamine, and gel filtration on AcA 54. The homogeneity

Evolution and structural diversification of Nictaba-like lectin genes in food crops with a focus on soybean (Glycine max).

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The Nictaba family groups all proteins that show homology to Nictaba, the tobacco lectin. So far, Nictaba and an Arabidopsis thaliana homologue have been shown to be implicated in the plant stress response. The availability of more than 50 sequenced plant genomes provided the opportunity for a

A genome-wide association study of a global rice panel reveals resistance in Oryza sativa to root-knot nematodes.

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The root-knot nematode Meloidogyne graminicola is one of the most serious nematode pests worldwide and represents a major constraint on rice production. While variation in the susceptibility of Asian rice (Oryza sativa) exists, so far no strong and reliable resistance has been reported. Quantitative

Induction of cytoplasmic mannose-binding jacalin-related lectins is a common phenomenon in cereals treated with jasmonate methyl ester.

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Treatment of whole plants with jasmonic acid methyl ester induces lectin activity in leaves of Oryza sativa, Hordeum vulgare, Triticum vulgare, Secale cereale and Zea mays. Purification and characterization of the lectins revealed that they all have a very similar molecular structure and

Expression of snowdrop lectin (GNA) in transgenic rice plants confers resistance to rice brown planthopper.

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Snowdrop lectin (Galanthus nivalis agglutinin; GNA) has been shown previously to be toxic towards rice brown planthopper (Nilaparvata lugens; BPH) when administered in artificial diet. BPH feeds by phloem abstraction, and causes 'hopper burn', as well as being an important virus vector. To evaluate

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