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Related Experiment Videos

Sequence and structural aspects of functional diversification in class I alpha-mannosidase evolution.

I K Jordan1, G R Bishop, D S Gonzalez

  • 1National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.

Bioinformatics (Oxford, England)
|October 24, 2001
PubMed
Summary

Natural selection drove the functional diversification of alpha-mannosidases, with key changes occurring at the protein periphery. This gradual evolution shaped distinct Endoplasmic Reticulum (ER) and Golgi enzyme groups.

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Class I alpha-mannosidases are a diverse family of glycoside hydrolases.
  • Phylogenetic analysis identified four distinct groups within this enzyme family.
  • Gene duplications contributed to the diversity of these enzymes since early eukaryotic evolution.

Purpose of the Study:

  • To investigate the role of natural selection in the divergence of Endoplasmic Reticulum (ER) and Golgi alpha-mannosidases.
  • To understand sequence and structural differences between phylogenetically and functionally distinct enzyme groups.

Main Methods:

  • Amino acid sequence alignment of the catalytic domain of class I alpha-mannosidases.
  • Phylogenetic analysis to identify enzyme groups.

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  • Comparison of site-specific amino acid variability profiles between ER and Golgi enzyme groups.

    • Main Results:

    • Statistically significant evidence for functional diversification at the sequence level between ER and Golgi groups.
    • Identified specific amino acid residues likely responsible for functional divergence.
    • Observed that many selected residues are located at the periphery of the catalytic domain, suggesting gradual functional adaptation.

    Conclusions:

    • Positive selection has driven functional diversification of alpha-mannosidases.
    • Peripheral residue changes, influenced by diversifying selection, likely contributed to gradual functional adaptation in ER and Golgi enzyme groups.
    • Findings support a Darwinian model of gradual natural selection in enzyme evolution.