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Glutelin subtype-dependent protein localization in rice grain evidenced by immunodetection analyses.
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GluA and GluB-4/5 glutelin subfamilies are mainly localized to outer region of the endosperm, particularly in its ventral side, in rice grain, but GluC is localized to throughout the endosperm. The major seed storage protein in rice (Oryza sativa) is glutelin, which forms a vacuole-derived protein
Structural Relationship among the Rice Glutelin Polypeptides.
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When the glutelin protein fraction of rice (Oryza sativa L.) seeds was fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, three size classes of proteins, 51 kilodaltons (kD), 34 to 37 kD, and 21 to 22 kD, as well as a contaminating prolamine polypeptide of 14 kD were
Variations in glutelin and high molecular weight endosperm proteins among subspecies of rice (Oryza sativa L.) detected by two-dimensional gel electrophoresis.
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Variations in endosperm polypeptides among 16 cultivars of rice were analyzed by two-dimensional gel electrophoresis. One glutelin alpha-subunit (alpha 8) with a molecular mass of 32.5 kDa was exclusively present in indica cultivars. By contrast, the glutelin alpha 3 subunit, with a molecular mass
Evaluation of the quality of a high-resistant starch and low-glutelin rice (Oryza sativa L.) generated through CRISPR/Cas9-mediated targeted mutagenesis
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A high-resistant starch (RS) and low-glutelin diet is beneficial for the health of patients with diabetes and kidney diseases. Rice is an important food crop worldwide. Previous studies demonstrated that downregulating the expression of rice starch branching enzyme IIb (SBEIIb) affected the
Diversity of rice glutelin polypeptides in wild species assessed by the higher-temperature sodium dodecyl sulfate-polyacrylamide gel electrophoresis and subunit-specific antibodies.
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In efforts to find genetic resources with high nutritional value of rice seed, we assessed the diversity of the major storage protein glutelin in 13 wild and 2 cultivated rice species by a unique SDS-PAGE method and subunit-specific antibodies. Maximum separation of microheterogeneous glutelin
Possible cleavage sites of glutelin partial degradation confirmed by immunological analysis in globulin-less mutants of rice (Oryza sativa L.).
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Proteolytic cleavage or partial degradation of proteins is one of the important post-translational modifications for various biological processes, but it is difficult to analyze. Previously, we demonstrated that some subunits of the major rice (Oryza sativa L.) seed storage protein glutelin are
Identification of 4-mercapto-4-methylpentan-2-one as the characteristic aroma of sake made from low-glutelin rice.
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The grassy characteristic aroma perceived in brewed sake made from low-glutelin rice (Oryza sativa L. Mizuhonoka) was examined by gas chromatography-olfactometry and gas chromatography-mass spectrometry. By comparing the odor properties and Kovats retention indices to those of standard compounds,
Expression pattern and activity of six glutelin gene promoters in transgenic rice.
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The shortage of strong endosperm-specific expression promoters for driving the expression of recombinant protein genes in cereal endosperm is a major limitation in obtaining the required level and pattern of expression. Six promoters of seed storage glutelin genes (GluA-1, GluA-2, GluA-3, GluB-3,
Structure and expression of the rice glutelin multigene family.
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A near full-length cDNA and three genomic clones for rice (Oryza sativa L.) glutelin were isolated and studied. Based on nucleic acid sequence and Southern blot analyses, the three isolated glutelin genomic clones were representative members of three gene subfamilies each containing five to eight
A rice (Oryza sativa L.) mutant having a low content of glutelin and a high content of prolamine.
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Among the mutant lines of rice that have been selected for morphological characters, one line, NM67, was found to have a low content of glutelin and a higher content of prolamine in its seed protein than other Japanese cultivars. This mutant is a semi-dwarf and partially sterile line, and its leaves
Accumulation of soybean glycinin and its assembly with the glutelins in rice
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Saline-soluble glycinins and insoluble glutelins are the major storage proteins in soybean (Glycine max) and rice (Oryza sativa), respectively. In spite of their differences in solubility properties, both proteins are members of the 11S globulin gene family based on their similarities in primary
Capillary electrophoresis for analysis of microheterogeneous glutelin subunits in rice (Oryza sativa L.).
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Glutelin, the major storage protein of rice seed, consists of microheterogenous subunits and partially exists in a macromolecular form that is polymerized by intersubunit disulfide bonds. In order to analyze the glutelin subunits using high-throughput CE, we first identified a sample preparation
Identification and variation of glutelin alpha polypeptides in the genus Oryza assessed by two-dimensional electrophoresis and step-by-step immunodetection.
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To obtain fundamental information for nutritional improvement of rice (Oryza sativa) seed proteins, the alpha polypeptides of the major storage protein glutelin varied over the genus Oryza were qualitatively and quantitatively characterized with unique methods. The polypeptides were maximally
Capillary electrophoresis of seed storage proteins: the separation and identification of microheterogeneous rice glutelin subunits.
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Glutelin, the major seed storage protein of rice (Oryza sativa L.), consists of multiple polymeric and monomeric subunits. Each subunit is composed of an α and a β polypeptide that are covalently linked by a disulfide bond. To analyze the microheterogeneous glutelin subunits using capillary
Expression pattern of UidA gene under the control of rice glutelin GluA-2 gene upstream sequence in transgenic rice endosperm.
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In order to study the expression pattern of rice glutelin endosperm specific promoter in Chinese cultivar Zhonghua 8 (Oryza sativa L. subsp japonica), UidA gene was fused with rice glutelin GluA-2 gene 5' upstream sequence 2.3 kb and 750 bp upstream respectively and transferred into rice by
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