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Current Topics in Plant Biology   Volumes    Volume 3 
Abstract
Recent progress in plant fucosylation
G. Costa, S. Lhernould, R. Léonard, F. Dupuy, L. Gastinel, A. Maftah
Pages: 101 - 111
Number of pages: 11
Current Topics in Plant Biology
Volume 3 

Copyright © 2002 Research Trends. All rights reserved

ABSTRACT

Pectins and hemicelluloses, arabinogalactan proteins and N-glycans biosynthesis are potential substrates for plant fucosyltransferases. So far, three classes of plant fucosyltransferases were described: the α2-FucT transferring Fuc on Gal residue of Polysaccharide, and the α3/4-FucT acting specifically on N-glycans. Until 1999, only one gene encoding an α2, α3 or α4 plant fucosyltranferase has been described. In Arabidopsis thaliana genome, 13 characterized or putative necleotidic sequences of FUT genes have been reported. The majority of them encode enzymes using polysaccharides as acceptor substrates such as xyloglucan (AtFUT1) and pectin or AGP (AtFuT2-10). Three Arabidopsis genes (AtFuT11, AtFuT12, AtFuT13) encode α 3/4-FucT and N-glycans for acceptor substrates. In plant, α2-fucosylation exhibited more gene diversity than α3/4- fucosylation. More than ten FUT genes control plant fucosylation processes, suggesting that Fuc-linkage is probably a key function such as the mammalian one.

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