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- Title
Biosynthesis of the carbohydrate moieties of arabinogalactan proteins by membrane‑bound β‑glucuronosyltransferases from radish primary roots
- Authors
Maya Endo; Toshihisa Kotake; Yoko Watanabe; Kazumasa Kimura; Yoichi Tsumuraya
- Abstract
A membrane fraction from etiolated 6-day-old primary radish roots (Raphanus sativus L. var hortensis) contained β-glucuronosyltransferases (GlcAT s) involved in the synthesis of the carbohydrate moieties of arabinogalactan proteins (AG Ps). The GlcAT s transferred [14C]GlcA from UDP-[14C]GlcA on to β-(1 → 3)-galactan as an exogenous acceptor substrate, giving a specific activity of 50–150 pmol min−1 (mg protein)−1. The enzyme specimen also catalyzed the transfer of [14C]GlcA on to an enzymatically modified AG P from mature radish root. Analysis of the transfer products revealed that the transfer of [14C]GlcA occurred preferentially on to consecutive (1 → 3)-linked β-Gal chains as well as single branched β-(1 → 6)-Gal residues through β-(1 → 6) linkages, producing branched acidic side chains. The enzymes also transferred [14C]GlcA residues on to several oligosaccharides, such as β- (1 → 6)- and β-(1 → 3)-galactotrioses. A trisaccharide, α-l-Araf-(1 → 3)-β-Gal-(1 → 6)-Gal, was a good acceptor, yielding a branched tetrasaccharide, α-l-Araf-(1 → 3) [β-GlcA-(1 → 6)]-β-Gal-(1 → 6)-Gal. We report the first in vitro assay system for β-GlcAT s involved in the AG synthesis as a step toward full characterization and cloning.
- Publication
Planta: An International Journal of Plant Biology, 2013, Vol 238, Issue 3, p1157
- ISSN
0032-0935
- Publication type
Article
- DOI
10.1007/s00425-013-1959-0