Glycobiology, Vol 9, 323-334, Copyright © 1999 by Oxford University Press
R Oriol, R Mollicone, A Cailleau, L Balanzino and C Breton
On the basis of function and sequence similarities, the vertebrate
fucosyltransferases can be classified into three groups: alpha-2-,
alpha-3-, and alpha-6-fucosyltransferases. Thirty new putative
fucosyltransferase genes from invertebrates and bacteria and six conserved
peptide motifs have been identified in DNA and protein databanks. Two of
these motifs are specific of alpha-3- fucosyltransferases, one is specific
of alpha-2-fucosyltransferases, another is specific of
alpha-6-fucosyltransferases, and two are shared by both alpha-2- and
alpha-6-fucosyltranserases. Based on these data, literature data, and the
phylogenetic analysis of the conserved peptide motifs, a model for the
evolution offucosyltransferase genes by successive duplications, followed
by divergent evolution is proposed, with either two different ancestors,
one for the alpha-2/6- fucosyltransferases and one for the
alpha-3-fucosyltransferases or a single common ancestor for the two
families. The expected properties of such an hypothetical ancestor suggest
that the plant or insect alpha-3- fucosyltransferases using chitobiose as
acceptor might be the present forms of this ancestor, since
fucosyltransferases using chitobiose as acceptor are expected to be of
earlier appearance in evolution than enzymes using N -acetyllactosamine.
However, an example of convergent evolution of fucosyltransferase genes is
suggested for the appearance of the Leaepitopes found in plants and
primates.
ORIGINAL ARTICLES
Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
INSERM U504, University of Paris South XI, 94807 Villejuif Cedex, France and CERMAV-CNRS, BP 53, 38041 Grenoble Cedex 9, France.
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