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Molecular Biology and Evolution 17:292-300 (2000)
© 2000 Society for Molecular Biology and Evolution


Articles

The {alpha}-Mannosidases: Phylogeny and Adaptive Diversification

Daniel S. Gonzalez* and I. King Jordan,{dagger}

*Department of Medical Microbiology, University of Georgia; and
{dagger}Department of Biological Sciences, University of Nevada at Las Vegas

{alpha}-Mannosidase enzymes comprise a class of gylcoside hydrolases involved in the maturation and degradation of glycoprotein-linked oligosaccharides. Various {alpha}-mannosidase enzymatic activities are encoded by an ancient and ubiquitous gene superfamily. A comparative sequence analysis was employed here to characterize the evolutionary relationships and dynamics of the {alpha}-mannosidase superfamily. A series of lineage-specific BLAST searches recovered the first ever recognized archaean and eubacterial {alpha}-mannosidase sequences, in addition to numerous eukaryotic sequences. Motif-based alignment and subsequent phylogenetic analysis of the entire superfamily revealed the presence of three well-supported monophyletic clades that represent discrete {alpha}-mannosidase families. The comparative method was used to evaluate the phylogenetic distribution of {alpha}-mannosidase functional variants within families. Results of this analysis demonstrate a pattern of functional diversification of {alpha}-mannosidase paralogs followed by conservation of function among orthologs. Nucleotide polymorphism among the most closely related pair of duplicated genes was analyzed to evaluate the role of natural selection in the functional diversification of {alpha}-mannosidase paralogs. Ratios of nonsynonymous and synonymous variation show an increase in the rate of nonsynonymous change after duplication and a relative excess of fixed nonsynonymous changes between the two groups of paralogs. These data point to a possible role for positive Darwinian selection in the evolution of {alpha}-mannosidase functional diversification following gene duplication.


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