ArticleNature communications2021
The adaptive landscape of a metallo-enzyme is shaped by environment-dependent epistasis.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Environment-dependent epistasis shapes adaptation to fluctuating resources.bioRxiv : the preprint server for biology · 2026Article
- How far can you go? Extrapolating values of catalytic activity from known protein landscapes in natural and directed evolution.Chemical Society reviews · 2026Review
- Single-molecule kinetic exploration of functional sub-states in an evolving phosphotriesterase.Nature communications · 2026Article
- Factors controlling protein evolvability-at the molecular scale.European biophysics journal : EBJ · 2026Article
- Epistatic drift in protein evolution.Current opinion in genetics & development · 2025Review
- Role of Php domain and related enzymes in the enzymatic degradation of G-series nerve agents.Molecular genetics and genomics : MGG · 2025Review
- Molecular complexity of the differential growth of freshwater diatoms along pH gradients.ISME communications · 2025Article
- The highly rugged yet navigable regulatory landscape of the bacterial transcription factor TetR.Nature communications · 2024Article
- The simplicity of protein sequence-function relationships.Nature communications · 2024Article
- Mechanistic conformational and substrate selectivity profiles emerging in the evolution of enzymes via parallel trajectories.Nature communications · 2024Article
- A combinatorially complete epistatic fitness landscape in an enzyme active site.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Discovery of a new bacterium, Microbacterium betulae sp. nov., in birch wood associated with hypersensitivity pneumonitis in woodworkers.Environmental microbiology reports · 2024Article
- Article
- The simplicity of protein sequence-function relationships.bioRxiv : the preprint server for biology · 2024Article
- Protein sequence landscapes are not so simple: on reference-free versus reference-based inference.bioRxiv : the preprint server for biology · 2024Article
- Pervasive epistasis exposes intramolecular networks in adaptive enzyme evolution.Nature communications · 2023Article
- Environment-dependent epistasis increases phenotypic diversity in gene regulatory networks.Science advances · 2023Article
- Robustness and innovation in synthetic genotype networks.Nature communications · 2023Article
- Experimental andACS infectious diseases · 2022Article
- Alternative design strategies to help build the enzymatic retrosynthesis toolbox.RSC chemical biology · 2022Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Enzymes can evolve new catalytic activity when environmental changes present them with novel substrates. Despite this seemingly straightforward relationship, factors other than the direct catalytic target can also impact adaptation. Here, we characterize the catalytic activity of a recently evolved bacterial methyl-parathion hydrolase for all possible combinations of the five functionally relevant mutations under eight different laboratory conditions (in which an alternative divalent metal is supplemented). The resultant adaptive landscapes across this historical evolutionary transition vary in terms of both the number of "fitness peaks" as well as the genotype(s) at which they are found as a result of genotype-by-environment interactions and environment-dependent epistasis. This suggests that adaptive landscapes may be fluid and molecular adaptation is highly contingent not only on obvious factors (such as catalytic targets), but also on less obvious secondary environmental factors that can direct it towards distinct outcomes.
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