Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase

FEBS Lett. 2008 Sep 22;582(21-22):3217-22. doi: 10.1016/j.febslet.2008.08.015. Epub 2008 Aug 26.

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-alpha-D-xylose onto methyl alpha-L-fucoside. The product formed was shown by 1D and 2D 1H NMR spectroscopy to be Me alpha-D-Xyl-(1,3)-alpha-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-alpha-L-fucopyranoside acted as an acceptor, although to a lesser extent than methyl alpha-L-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis Proteins / classification
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Cloning, Molecular
  • Fucose / metabolism
  • Genes, Plant
  • Pectins / metabolism*
  • Pentosyltransferases / classification
  • Pentosyltransferases / genetics
  • Pentosyltransferases / metabolism*
  • Phylogeny
  • Pichia / genetics
  • Substrate Specificity
  • UDP Xylose-Protein Xylosyltransferase

Substances

  • Arabidopsis Proteins
  • rhamnogalacturonan II
  • Fucose
  • Pectins
  • Pentosyltransferases