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http://purl.uniprot.org/citations/30082766http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30082766http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30082766http://www.w3.org/2000/01/rdf-schema#comment"Pectin is one of the three key cell wall polysaccharides in land plants and consists of three major structural domains: homogalacturonan, rhamnogalacturonan I (RG-I) and RG-II. Although the glycosyltransferase required for the synthesis of the homogalacturonan and RG-II backbone was identified a decade ago, those for the synthesis of the RG-I backbone, which consists of the repeating disaccharide unit [→2)-α-L-Rha-(1 → 4)-α-D-GalUA-(1→], have remained unknown. Here, we report the identification and characterization of Arabidopsis RG-I:rhamnosyltransferases (RRTs), which transfer the rhamnose residue from UDP-β-L-rhamnose to RG-I oligosaccharides. RRT1, which is one of the four Arabidopsis RRTs, is a single-spanning transmembrane protein, localized to the Golgi apparatus. RRT1 was highly expressed during formation of the seed coat mucilage, which is a specialized cell wall with abundant RG-I. Loss-of-function mutation in RRT1 caused a reduction in the level of RG-I in the seed coat mucilage. The RRTs belong to a novel glycosyltransferase family, now designated GT106. This is a large plant-specific family, and glycosyltransferases in this family seem to have plant-specific roles, such as biosynthesis of plant cell wall polysaccharides."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.org/dc/terms/identifier"doi:10.1038/s41477-018-0217-7"xsd:string
http://purl.uniprot.org/citations/30082766http://purl.org/dc/terms/identifier"doi:10.1038/s41477-018-0217-7"xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kato K."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kato K."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Hara-Nishimura I."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Hara-Nishimura I."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Takenaka Y."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Takenaka Y."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Takeda Y."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Takeda Y."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Takeda A."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Takeda A."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kuroha T."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kuroha T."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kajiura H."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kajiura H."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kunieda T."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Kunieda T."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Matsubayashi Y."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Matsubayashi Y."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Ogawa-Ohnishi M."xsd:string
http://purl.uniprot.org/citations/30082766http://purl.uniprot.org/core/author"Ogawa-Ohnishi M."xsd:string