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Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

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Published on: January 16, 2016

The relationship between relative solvent accessibility and evolutionary rate in protein evolution.

Duncan C Ramsey1, Michael P Scherrer, Tong Zhou

  • 1Center for Computational Biology and Bioinformatics, Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712, USA.

Genetics
|April 7, 2011
PubMed
Summary

Scientists developed a mathematical model linking protein evolutionary rates to amino acid distributions. This model accurately reflects the relationship between site evolutionary rates and relative solvent accessibility (RSA) in proteins.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biophysics

Background:

  • A linear relationship exists between evolutionary rates of sites and relative solvent accessibility (RSA) in Saccharomyces cerevisiae.
  • Understanding the biophysical basis of this relationship is crucial for evolutionary studies.

Purpose of the Study:

  • To develop a mathematical model that accurately reproduces the observed linear relationship between evolutionary rates and RSA.
  • To investigate the role of site-specific amino acid distributions in this relationship.

Main Methods:

  • Evaluation of two proposed models: one based on selection strength correlating with RSA, and another on RSA-dependent amino acid distributions.
  • Development and testing of a novel model based on observed site-specific amino acid distributions.

Main Results:

  • The two initially proposed models failed to reproduce the observed linear relationship.
  • The newly developed model, based on site-specific amino acid distributions, successfully reproduced the observed relationship.

Conclusions:

  • Evolutionary rates are directly linked to the distribution of amino acids at individual protein sites.
  • Further insights into biophysical mechanisms governing amino acid distributions will enhance understanding of evolutionary rates.