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Related Experiment Videos

Excessive homoplasy in an evolutionarily constrained protein

R S Wells1

  • 1Museum of Comparative Zoology Laboratories, Harvard University, Cambridge, Massachusetts 02138, USA.

Proceedings. Biological Sciences
|April 22, 1996
PubMed
Summary

Investigating the glycerol-3-phosphate dehydrogenase (Gpdh) in Drosophila revealed constrained evolution. Four specific sites exhibit unusual high rates of change, showing a novel pattern of evolutionary "flip-flopping" between amino acid states.

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Area of Science:

  • Evolutionary biology
  • Molecular evolution
  • Genomics

Background:

  • The evolution of conserved proteins across closely related species is not well understood.
  • Glycerol-3-phosphate dehydrogenase (Gpdh) is a crucial enzyme involved in metabolic pathways.

Purpose of the Study:

  • To investigate the evolutionary patterns of the Gpdh locus in Drosophila species.
  • To identify the forces shaping the evolution of monomorphic proteins.

Main Methods:

  • Sequencing of the Gpdh locus across a wide range of Drosophila species.
  • Phylogenetic analysis of the Gpdh sequences.
  • Comparison of Gpdh evolution with other proteins.

Main Results:

  • Purifying selection is the primary force acting on Gpdh evolution, but amino acid replacements do occur.

Related Experiment Videos

  • A high proportion of amino acid parallelism and reversal (homoplasy) was observed at four specific sites.
  • These four sites evolve at a significantly higher rate than other variable positions, exhibiting a unique pattern of "flip-flopping" between two amino acid states.

    • Conclusions:

    • Gpdh evolution is strongly constrained, with limited amino acid variation allowed.
    • A novel class of hypervariable sites, characterized by rapid "flip-flopping" between two states, has been identified.
    • These findings provide new insights into the mechanisms of protein evolution under constraint.