Selection enhances protein evolvability by increasing mutational robustness and foldability

Author:

Zheng Jia12ORCID,Guo Ning3ORCID,Wagner Andreas124ORCID

Affiliation:

1. Department of Evolutionary Biology and Environmental Studies, University of Zurich, Zurich, Switzerland.

2. Swiss Institute of Bioinformatics, Quartier Sorge-Batiment Genopode, Lausanne, Switzerland.

3. Zwirnereistrasse 11, Wallisellen, Zurich, Switzerland.

4. The Santa Fe Institute, Santa Fe, NM, USA.

Abstract

Selection enhances mutation toleration Mutations generate variability that is either neutral or subject to natural selection. Robustness is a measure of the ability to withstand deleterious mutational effects. Zheng et al. exposed Escherichia coli populations expressing a yellow fluorescent protein to strong, weak, or no selection for yellow fluorescence for four generations. They then selected these populations to a related function, green fluorescence, for four more generations. The strong selection first for yellow and then green fluorescence resulted in the most green fluorescence and the accumulation of the most mutations. This outcome likely was due to the increased foldability of the protein. Selection thus provides a threshold for mutation accumulation, but robustness maintains a buffer necessary for protein evolution. Science , this issue p. eabb5962

Funder

European Research Council

Swiss National Science Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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