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Secreted Proteins Defy the Expression Level-Evolutionary Rate Anticorrelation.

Felix Feyertag1, Patricia M Berninsone1, David Alvarez-Ponce1

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Molecular Biology and Evolution
|December 24, 2016
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Summary

Protein evolution rates are linked to expression levels, but secreted proteins show no such correlation. This suggests that the secretory pathway and extracellular location reduce the costs of protein misfolding and interactions, impacting evolutionary rates.

Keywords:
E–R anticorrelationdN/dSexpression levelsrates of evolutionsecreted proteins.

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Genomics

Background:

  • Protein expression levels strongly correlate with evolutionary rates across organisms, known as the expression-rate (E-R) anticorrelation.
  • This anticorrelation is often attributed to fitness costs associated with protein misfolding and non-specific interactions, which increase with protein abundance.
  • Secreted proteins undergo specialized folding in the endoplasmic reticulum and function extracellularly, potentially altering these fitness costs.

Purpose of the Study:

  • To investigate whether the secretory pathway and extracellular location mitigate the E-R anticorrelation.
  • To determine if secreted proteins exhibit different evolutionary rate patterns compared to intracellular proteins.

Main Methods:

  • Analysis of protein abundance and evolutionary rates in human proteomes.
  • Examination of protein abundance data across multiple human tissues.
  • Comparative analysis of mRNA abundance and E-R correlation in various model organisms (C. elegans, E. coli, D. melanogaster, S. cerevisiae, A. thaliana).

Main Results:

  • Human secreted proteins show no correlation between evolutionary rates and protein abundance.
  • This finding remains robust after controlling for confounding factors and across different human tissues.
  • The E-R correlation is consistently weaker (less negative or nonsignificant) in secreted proteins across multiple species.

Conclusions:

  • The specialized environment of the secretory pathway and extracellular space reduces the fitness consequences of protein misfolding and interactions.
  • These factors weaken or abolish the typical E-R anticorrelation observed for intracellular proteins.
  • Understanding these mechanisms provides insights into the drivers of protein evolution.