| Literature DB >> 30082766 |
Yuto Takenaka1, Kohei Kato2, Mari Ogawa-Ohnishi3, Kana Tsuruhama2, Hiroyuki Kajiura2, Kenta Yagyu2, Atsushi Takeda1,2, Yoichi Takeda2, Tadashi Kunieda4,5, Ikuko Hara-Nishimura4, Takeshi Kuroha6, Kazuhiko Nishitani6, Yoshikatsu Matsubayashi3, Takeshi Ishimizu7,8.
Abstract
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.Entities:
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Year: 2018 PMID: 30082766 DOI: 10.1038/s41477-018-0217-7
Source DB: PubMed Journal: Nat Plants ISSN: 2055-0278 Impact factor: 15.793