Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase
Research output: Contribution to journal › Journal article › Research › peer-review
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 (1)H 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.
Original language | English |
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Journal | FEBS Letters |
Volume | 582 |
Issue number | 21-22 |
Pages (from-to) | 3217-3222 |
Number of pages | 6 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 2008 |
Bibliographical note
Author KEYWORDS: rhamnogalacturonan II; pectin; GT-family-77; xylosyltransferase; Pichia pastoris
KEYWORDS Plus: MOLECULAR CHARACTERIZATION; ARABIDOPSIS; BIOSYNTHESIS; XYLOGLUCAN; SYNTHASE; PECTIN; GENES; IDENTIFICATION; FAMILY; GALACTOSYLTRANSFERASE
ID: 6709055