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Published on: October 23, 2016
The effect of chaperonin buffering on protein evolution
Tom A Williams1, Mario A Fares
1Department of Genetics, University of Dublin, Trinity College, Dublin, Ireland.
Genome Biology and Evolution
|July 28, 2010
Summary
Molecular chaperones like GroEL buffer mutations, increasing client protein evolution rates. Loss of GroEL in Mycoplasmas shows clients adapt, demonstrating chaperonin impact on proteome evolution.
Area of Science:
- Evolutionary biology
- Molecular biology
- Biochemistry
Background:
- Molecular chaperones, such as Hsp90 and GroEL, are vital for protein folding and can buffer phenotypic variation.
- Previous studies suggest chaperonins like E. coli GroEL facilitate the evolution of client proteins with destabilizing mutations.
Purpose of the Study:
- To investigate the evolutionary significance of chaperonin-mediated buffering of protein mutations.
- To quantify the impact of GroEL buffering on the evolutionary rate of client proteins in E. coli.
- To examine the evolutionary trajectory of GroEL client proteins in Mycoplasmas, organisms lacking chaperonins.
Main Methods:
- Modeling the per-residue evolutionary rate of the crystallized E. coli proteome.
- Analyzing the contributions of chaperonin buffering, functional importance, and structural features (e.g., residue contact density).
- Evaluating the effect of GroEL loss on client protein evolution in 11 Mycoplasma species.
Main Results:
- GroEL buffering of deleterious mutations accelerates the evolutionary rate of client proteins.
- In Mycoplasmas, the loss of GroEL was followed by client proteins losing their obligate dependency on it.
- Chaperonins significantly influence proteome evolution by modulating protein folding.
Conclusions:
- Chaperonin-mediated buffering is a significant evolutionary force, impacting protein evolution rates.
- The loss of GroEL in Mycoplasmas demonstrates the adaptability of client proteins to altered folding requirements.
- Individual molecular chaperones play a crucial role in shaping the evolution of entire proteomes.
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