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Reverse evolution leads to genotypic incompatibility despite functional and active site convergence.

Miriam Kaltenbach1, Colin J Jackson2, Eleanor C Campbell2

  • 1Michael Smith Laboratories, University of British Columbia, Vancouver, Canada.

Elife
|August 15, 2015
PubMed
Summary

Enzyme evolution can be phenotypically reversible, restoring function via new mutations. However, genotypic irreversibility and sequence incompatibility mean the exact original state is not regained, highlighting enzyme adaptive landscapes.

Keywords:
E. colibiochemistryenzyme evolutionevolutionary biologyevolutionary reversibilitygenomicslaboratory evolutionmutational epistasissequence incompatibilitysequence-structure-function relationship

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Understanding enzyme evolution reversibility is key to the protein sequence-structure-function relationship.
  • Directed evolution experiments test the boundaries of enzyme adaptability and historical contingency.

Purpose of the Study:

  • To experimentally test the reversibility of enzyme evolution.
  • To investigate the molecular basis of evolutionary pathways using directed evolution.
  • To explore enzyme sequence-structure-function relationships under evolutionary pressure.

Main Methods:

  • Directed evolution was used to convert a phosphotriesterase to an arylesterase and then back to a phosphotriesterase.
  • Mutational analysis and activity assays were employed to assess enzyme function.
  • Epistasis and sequence compatibility were examined to understand genotypic constraints.

Main Results:

  • Wild-type phosphotriesterase function was restored with a >10(4)-fold activity increase, but through an alternative mutation set.
  • The enzyme active site converged to its original state, driven by catalytic requirements.
  • Extensive epistasis and sequence incompatibility demonstrated genotypic irreversibility despite phenotypic reversibility.

Conclusions:

  • Enzyme evolution is phenotypically reversible but genotypically irreversible.
  • Catalytic requirements impose evolutionary constraints, leading to active site convergence.
  • The enzyme's adaptive landscape is rugged, with distinct fitness peaks for different functional sequences.