Molecular Biology and Evolution 19:1451-1463 (2002)
© 2002 Society for Molecular Biology and Evolution
Common Origin and Evolution of Glycosyltransferases Using Dol-P-monosaccharides as Donor Substrate
INSERM U504, University of Paris Sud XI, Villejuif, France
On the basis of the analysis of 64 glycosyltransferases from 14 species we propose that several successive duplications of a common ancestral gene, followed by divergent evolution, have generated the mannosyltransferases and the glucosyltransferases involved in asparagine-linked glycosylation (ALG) and phosphatidyl-inositol glycan anchor (PIG or GPI), which use lipid-related donor and acceptor substrates. Long and short conserved peptide motifs were found in all enzymes. Conserved and identical amino acid positions were found for the 
2/6- and the 3/4-mannosyltransferases and for the 2/3-glucosyltransferases, suggesting unique ancestors for these three superfamilies. The three members of the 2-mannosyltransferase family (ALG9, PIG-B, and SMP3) and the two members of the 3-glucosyltransferase family (ALG6 and ALG8) shared 11 and 30 identical amino acid positions, respectively, suggesting that these enzymes have also originated by duplication and divergent evolution. This model predicts a common genetic origin for ALG and PIG enzymes using dolichyl-phospho-monosaccharide (Dol-P-monosaccharide) donors, which might be related to similar spatial orientation of the hydroxyl acceptors. On the basis of the multiple sequence analysis and the prediction of transmembrane topology we propose that the endoplasmic reticulum glycosyltransferases using Dol-P-monosaccharides as donor substrate have a multispan transmembrane topology with a first large luminal conserved loop containing the long motif and a small cytosolic conserved loop containing the short motif, different from the classical type II glycosyltransferases, which are anchored in the Golgi by a single transmembrane domain.
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