Abstract
An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of d-xylose from UDP-α- d-xylose onto methyl α- l-fucoside. The product formed was shown by 1D and 2D 1H NMR spectroscopy to be Me α- d-Xyl-(1,3)-α- l-Fuc, which is identical to the proposed target structure in the A-chain of rhamnogalacturonan II. Chemically synthesized methyl l-fucosides derivatized by methyl groups on either the 2-, 3- or 4 position were tested as acceptor substrates but only methyl 4- O-methyl-α- l-fucopyranoside acted as an acceptor, although to a lesser extent than methyl α- l-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase.
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