ArticleNature ecology & evolution2022
Low protein expression enhances phenotypic evolvability by intensifying selection on folding stability.
Article in Nature ecology & evolution, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Molecular evolution in light of regulatory-coding epistasis.EMBO reports · 2026Review
- Mistranslation suppresses mistranscription in eukaryotes.Nature communications · 2026Article
- Neutral drift upon threshold-like selection promotes variation in antibiotic resistance phenotype.Nature communications · 2024Article
- Rapid evolutionary change in trait correlations of single proteins.Nature communications · 2024Article
- Epistasis between promoter activity and coding mutations shapes gene evolvability.Science advances · 2023Article
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Authors and funding
4 authors at 2 institutions in 4 countries.
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Abstract
Protein abundance affects the evolution of protein genotypes, but we do not know how it affects the evolution of protein phenotypes. Here we investigate the role of protein abundance in the evolvability of green fluorescent protein (GFP) towards the novel phenotype of cyan fluorescence. We evolve GFP in E. coli through multiple cycles of mutation and selection and show that low GFP expression facilitates the evolution of cyan fluorescence. A computational model whose predictions we test experimentally helps explain why: lowly expressed proteins are under stronger selection for proper folding, which facilitates their evolvability on short evolutionary time scales. The reason is that high fluorescence can be achieved by either few proteins that fold well or by many proteins that fold less well. In other words, we observe a synergy between a protein's scarcity and its stability. Because many proteins meet the essential requirements for this scarcity-stability synergy, it may be a widespread mechanism by which low expression helps proteins evolve new phenotypes and functions.
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