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Related Experiment Video

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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Disulfide Bonds Enable Accelerated Protein Evolution.

Felix Feyertag1, David Alvarez-Ponce1

  • 1Department of Biology, University of Nevada-Reno, Reno, NV.

Molecular Biology and Evolution
|April 22, 2017
PubMed
Summary
This summary is machine-generated.

Disulfide bonds accelerate protein evolution by increasing stability, allowing sequences to change faster. This effect was observed in membrane and extracellular proteins, but not the longest ones.

Keywords:
dN/dSdisulfide bridgesrates of evolution

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Protein evolution rates vary significantly across different proteomes.
  • The factors driving this evolutionary rate variability remain largely unknown.
  • Protein structure and stability are critical determinants of evolutionary trajectories.

Purpose of the Study:

  • To investigate the role of disulfide bonds in protein sequence evolution.
  • To test the hypothesis that disulfide bonds act as buffers against deleterious mutations, thereby accelerating evolution.
  • To determine if disulfide bonds influence the rate of molecular evolution in different protein types.

Main Methods:

  • Comparative analysis of protein sequences and evolutionary rates.
  • Statistical examination of proteins with and without disulfide bonds.
  • Multivariate analyses to control for confounding factors.
  • Investigation of positive selection signatures in protein-coding genes.

Main Results:

  • Proteins with disulfide bonds evolved significantly faster than those without.
  • Membrane proteins with disulfide bonds showed an 88% accelerated evolution rate.
  • Extracellular proteins with disulfide bonds evolved 49% faster.
  • Genes encoding disulfide-bonded proteins displayed higher rates of positive selection.
  • This trend was independent of protein length, except for the longest proteins.

Conclusions:

  • Disulfide bonds enhance protein stability, decoupling structure from sequence and facilitating faster evolution.
  • The presence of disulfide bonds is a significant factor contributing to accelerated molecular evolution.
  • Alternative stabilization mechanisms in very long proteins may obviate the need for disulfide bonds in buffering mutations.