Widespread gene conversion of alpha-2-fucosyltransferase genes in mammals

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Title Widespread gene conversion of alpha-2-fucosyltransferase genes in mammals
Author Abrantes, Joana; Posada, David; Guillon, Patrice Michel Guy; Esteves, Pedro J.; Pendu, Jacques Le
Journal Name Journal of molecular evolution
Year Published 2009
Place of publication Berlin, Germany
Publisher Springer-Verlag
Abstract The alpha-2-fucosyltransferases (alpha2FTs) are enzymes involved in the biosynthesis of alpha2fucosylated glycan structures. In mammalian genomes, there are three alpha2FT genes located in tandem-FUT1, FUT2, and Sec1-each contained within a single exon. It has been suggested that these genes originated from two successive duplications, with FUT1 being generated first and FUT2 and Sec1 second. Despite gene conversion being considered the main mechanism of concerted evolution in gene families, previous studies of primates alpha2FTs failed to detect it, although the occurrence of gene conversion between FUT2 and Sec1 was recently reported in a human allele. The primary aim of our work was to initiate a broader study on the molecular evolution of mammalian alpha2FTs. Sequence comparison leads us to confirm that the three genes appeared by two rounds of duplication. In addition, we were able to detect multiple gene-conversion events at the base of primates and within several nonprimate species involving FUT2 and Sec1. Gene conversion involving FUT1 and either FUT2 or Sec1 was also detected in rabbit. The extent of gene conversion between the alpha2FTs genes appears to be species-specific, possibly related to functional differentiation of these genes. With the exception of rabbits, gene conversion was not observed in the region coding the C-terminal part of the catalytic domain. In this region, the number of amino acids that are identical between FUT1 and FUT2, but different in Sec1, is higher than in other parts of the protein. The biologic meaning of this observation may be related to functional constraints.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1007/s00239-009-9239-0
Volume 69
Issue Number 1
Page from 22
Page to 31
ISSN 0022-2844
Date Accessioned 2010-07-27
Language en_AU
Faculty Faculty of Science, Environment, Engineering and Technology
Subject Host-Parasite Interactions
URI http://hdl.handle.net/10072/34401
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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