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Related Experiment Videos

The selection of acceptable protein mutations.

Rajkumar Sasidharan1, Cyrus Chothia

  • 1Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, United Kingdom. rajkumar.sasidharan@yale.edu

Proceedings of the National Academy of Sciences of the United States of America
|June 2, 2007
PubMed
Summary
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Protein sequence divergence is governed by general constraints that vary with evolutionary distance. These constraints affect mutation rates in different protein regions, explaining structure-sequence divergence relationships.

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Bioinformatics

Background:

  • Proteins with conserved structure and function exhibit sequence divergence.
  • Understanding constraints on protein evolution is crucial for predicting functional changes.

Purpose of the Study:

  • To determine general constraints governing sequence divergence in proteins with conserved structure and function.
  • To investigate how these constraints vary with evolutionary divergence.

Main Methods:

  • Collected and analyzed orthologous sequences from humans/mice, humans/chickens, and Escherichia coli/Salmonella enterica.
  • Categorized sequence pairs based on sequence identity and divergence.
  • Examined mutation distribution across buried, intermediate, and exposed protein regions.

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Main Results:

  • Strikingly similar patterns of mutation frequency and rank order were observed across diverse taxonomic groups.
  • The range of common mutations expanded similarly with increasing divergence in all groups.
  • Mutation rates varied across protein regions (buried, intermediate, exposed) with increasing divergence, explaining exponential structure-sequence divergence.

Conclusions:

  • General, well-defined constraints govern protein sequence divergence.
  • The nature of these constraints changes with evolutionary divergence.
  • These findings explain the relationship between protein structure and sequence divergence.