fucose/oryza sativa

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N-glycan containing a core α1,3-fucose residue is required for basipetal auxin transport and gravitropic response in rice (Oryza sativa).

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In plants, α1,3-fucosyltransferase (FucT) catalyzes the transfer of fucose from GDP-fucose to asparagine-linked GlcNAc of the N-glycan core in the medial Golgi. To explore the physiological significance of this processing, we isolated two Oryza sativa (rice) mutants (fuct-1 and fuct-2) with loss of

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

Identification and Localization of Sugar Components of Rice (Oryza sativa L.) Root Cap Mucilage.

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This study is devoted to the neutral sugar analysis of rice root exudate and root cap mucilage.The results indicate that most of the carbohydrate in the exudate is released in soluble dialysable form, mainly as glucose. Mucilage polymers represent only a minor fraction of the whole exudate

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

Bacterial Stripe of Hog Millet Caused by Acidovorax avenae subsp. avenae, a New Disease in Korea.

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In July 2011, bacterial stripe was observed on a commercial field of hog millet (Panicum miliaceum L.) in Chuncheon, Korea, with a disease incidence of 37% in the field. Symptoms on leaves included reddish-brown, long, narrow stripes that varied in length and were sharply delineated by uninfected

N-Glycomic and Microscopic Subcellular Localization Analyses of NPP1, 2 and 6 Strongly Indicate that trans-Golgi Compartments Participate in the Golgi to Plastid Traffic of Nucleotide Pyrophosphatase/Phosphodiesterases in Rice.

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Nucleotide pyrophosphatase/phosphodiesterases (NPPs) are widely distributed N-glycosylated enzymes that catalyze the hydrolytic breakdown of numerous nucleotides and nucleotide sugars. In many plant species, NPPs are encoded by a small multigene family, which in rice are referred to NPP1-NPP6

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