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Daily Transfers, Archiving Populations, and Measuring Fitness in the Long-Term Evolution Experiment with Escherichia coli
Published on: August 18, 2023
Protein robustness promotes evolutionary innovations on large evolutionary time-scales
Evandro Ferrada1, Andreas Wagner
1Department of Biochemistry, University of Zurich, Building Y27, Winterthurerstrasse 190, 8057 Zurich, Switzerland. e.ferrada@bioc.uzh.ch
Proceedings. Biological Sciences
|April 24, 2008
Summary
Molecules that can evolve neutrally, or are robust, are better at generating evolutionary innovations over long timescales. This protein robustness is linked to functional diversity and innovation capacity.
Area of Science:
- Evolutionary biology
- Molecular evolution
- Biochemistry
Background:
- Laboratory experiments suggest neutral evolution aids molecular innovation.
- Life's evolutionary processes occur over billions of years.
- The role of neutral evolution in long-term innovation remains less understood.
Purpose of the Study:
- To investigate if molecular robustness (neutral evolvability) facilitates evolutionary innovation on geological timescales.
- To link protein designability to neutral evolution and functional innovation.
Main Methods:
- Utilized protein designability as a proxy for a protein structure's capacity for neutral evolution.
- Assessed functional innovation using catalytic diversity and gene ontology molecular functional diversity.
- Examined associations between designability, folding rate, and intrinsic disorder.
Main Results:
- Proteins with higher designability (greater neutral evolvability) exhibit a superior capacity for generating functional innovations.
- Demonstrated a positive correlation between protein robustness and the potential for evolutionary innovation.
- Identified significant links between structural designability, folding rates, and intrinsic disorder.
Conclusions:
- Molecular robustness is crucial for facilitating evolutionary innovation across vast timescales.
- Protein designability serves as a reliable indicator of a protein's potential for long-term evolutionary innovation.
- Structural factors like folding rate and intrinsic disorder intricately influence protein evolution and innovation.
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