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A Mutation-Selection Model of Protein Evolution under Persistent Positive Selection.

Asif U Tamuri1,2, Mario Dos Reis3

  • 1Centre for Advanced Research Computing, University College London, London, United Kingdom.

Molecular Biology and Evolution
|October 25, 2021
PubMed
Summary
This summary is machine-generated.

We developed a new model for protein evolution under persistent positive selection (PPS). This method directly estimates selection coefficients, improving the detection of molecular adaptation in proteins like RuBisCO and influenza HA.

Keywords:
RuBisCOcytochrome bdistribution of fitness effectsinfluenzamutation–selection modelpositive selection

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Area of Science:

  • Evolutionary biology
  • Population genetics
  • Molecular evolution

Background:

  • Persistent positive selection (PPS) drives protein evolution during environmental changes, adaptive radiations, and host-pathogen interactions.
  • Traditional methods using the ratio of substitution rates (ω > 1) may be conservative due to deleterious mutations at selected sites.

Purpose of the Study:

  • To model protein evolution under persistent positive selection (PPS) using first principles of population genetics.
  • To develop a more accurate method for detecting molecular adaptation by directly estimating selection coefficients.

Main Methods:

  • Developed a mutation-selection model for protein evolution under PPS, treating it as an irreversible Markov process.
  • Implemented a penalized-likelihood approach to estimate selection coefficients directly at protein sites.
  • Applied the model to detect PPS in plant RuBisCO and influenza HA proteins.

Main Results:

  • Protein evolution under PPS exhibits a strongly asymmetrical distribution of selection coefficients.
  • The model demonstrates that the ω > 1 criterion is conservative and arbitrary.
  • Successfully detected PPS in plant RuBisCO and influenza HA proteins using the new method.

Conclusions:

  • Direct estimation of selection coefficients provides a more robust approach to detecting molecular adaptation than using ω.
  • The new model enhances the ability to identify evolutionary adaptation in proteins under persistent positive selection.