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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Positive selection differs between protein secondary structure elements in Drosophila.

Kate E Ridout1, Christopher J Dixon, Dmitry A Filatov

  • 1Department of Plant Sciences, University of Oxford, Oxford, United Kingdom.

Genome Biology and Evolution
|July 14, 2010
PubMed
Summary
This summary is machine-generated.

Protein secondary structures influence evolution. Disordered regions, like random coils, experience more positive selection, while ordered structures like helices and beta-sheets are less adaptable.

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Genomics

Background:

  • Protein secondary structures possess distinct physicochemical properties and functional roles.
  • The impact of protein structure on the action of Darwinian selection at the amino acid level remains poorly understood.

Purpose of the Study:

  • To investigate the relationship between protein secondary structure and positive selection.
  • To determine how structural organization influences molecular adaptation.

Main Methods:

  • Phylogeny-based likelihood tests were employed to detect positive selection.
  • Analysis was conducted across six species of Drosophila.

Main Results:

  • Amino acids in disordered regions (random coils) showed significantly higher rates of positive selection than expected.
  • Residues in helical and beta-sheet structures exhibited lower positive selection than predicted.
  • Positively selected sites were found to cluster in protein sequences and were more frequent toward gene ends.

Conclusions:

  • Highly organized and hydrophobic structures (helices, beta-structures) are less tolerant to molecular adaptation.
  • Disordered, hydrophilic regions are more flexible and adaptable under evolutionary pressure.
  • Protein structure plays a critical role in modulating the efficacy of selection at the amino acid level.