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Molecular clock in neutral protein evolution.

Claus O Wilke1

  • 1Keck Graduate Institute of Applied Life Sciences, 535 Watson Drive, Claremont, California 91711, USA. wilke@kgi.edu

BMC Genetics
|August 31, 2004
PubMed
Summary
This summary is machine-generated.

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The molecular clock in protein evolution is overdispersed for small mutation rates and population sizes. For larger mutation rates and population sizes, the molecular clock becomes more Poissonian, approaching a steady rate.

Area of Science:

  • Molecular Evolution
  • Computational Biology
  • Biophysics

Background:

  • Amino-acid substitution rates often exhibit an index of dispersion > 1, known as the overdispersed molecular clock.
  • Previous models explained this by proteins getting trapped in low-neutrality regions, suppressing substitution rates.
  • These models were limited to small mutation rate (μ) and population size (Ne) products (μNe).

Purpose of the Study:

  • Investigate the behavior of the molecular clock in silico protein evolution across varying μNe.
  • Determine how substitution rate dynamics change with different mutation rates and population sizes.

Main Methods:

  • In silico protein evolution simulations.
  • Analysis of the index of dispersion as a function of μNe.

Related Experiment Videos

  • Exploration of selective pressures influencing protein evolution.

    • Main Results:

    • The index of dispersion decreases as μNe increases, approaching 1 for large μNe.
    • This stabilization is attributed to selection for mutational robustness at high μNe.
    • Mutational robustness prevents populations from entering low-neutrality traps, steadying the molecular clock.

    Conclusions:

    • Neutral protein evolution exhibits two regimes: strongly overdispersed for small μNe and Poissonian for large μNe.
    • The overdispersed regime applies to most plants and animals.
    • The Poissonian regime may be relevant for RNA viruses.