ArticleProceedings of the National Academy of Sciences of the United States of America2005
On the conservative nature of intragenic recombination.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 121 citations in OpenAlex.
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- Dynamic signature of activity-stability tradeoff in lactamase evolution.Nature communications · 2026Article
- Genetic Evolution Between HIV-1 Groups M and O: HIV-1/MO Recombinant Forms.Journal of medical virology · 2025Review
- Enriching productive mutational paths accelerates enzyme evolution.Nature chemical biology · 2024Article
- Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering.ACS central science · 2024Review
- Hyper-diverse antigenic variation and resilience to transmission-reducing intervention in falciparum malaria.medRxiv : the preprint server for health sciences · 2024Article
- Sequence-activity mapping via depletion reveals striking mutational tolerance and elucidates functional motifs in Tur1a antimicrobial peptide.Protein engineering, design & selection : PEDS · 2024Article
- Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange.Protein science : a publication of the Protein Society · 2023Article
- LibGENiE - A bioinformatic pipeline for the design of information-enriched enzyme libraries.Computational and structural biotechnology journal · 2023Article
- Identification of TFPI as a receptor reveals recombination-driven receptor switching in Clostridioides difficile toxin B variants.Nature communications · 2022Article
- Experimental exploration of a ribozyme neutral network using evolutionary algorithm and deep learning.Nature communications · 2022Article
- Conserved recombination patterns across coronavirus subgenera.Virus evolution · 2022Article
- Cross-species transmission, evolution and zoonotic potential of coronaviruses.Frontiers in cellular and infection microbiology · 2022Review
- Quantifying the Mutational Robustness of Protein-Coding Genes.Journal of molecular evolution · 2021Article
- An antigenic diversification threshold for falciparum malaria transmission at high endemicity.PLoS computational biology · 2021Article
- Directed evolution methods for overcoming trade-offs between protein activity and stability.AIChE journal. American Institute of Chemical Engineers · 2020Article
- A Continuing Career in Biocatalysis: Frances H. Arnold.ACS catalysis · 2019Article
- Machine-learning-guided directed evolution for protein engineering.Nature methods · 2019Review
- Evolution of a novel chimeric maltotriose transporter in Saccharomyces eubayanus from parent proteins unable to perform this function.PLoS genetics · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Intragenic recombination rapidly creates protein sequence diversity compared with random mutation, but little is known about the relative effects of recombination and mutation on protein function. Here, we compare recombination of the distantly related beta-lactamases PSE-4 and TEM-1 to mutation of PSE-4. We show that, among beta-lactamase variants containing the same number of amino acid substitutions, variants created by recombination retain function with a significantly higher probability than those generated by random mutagenesis. We present a simple model that accurately captures the differing effects of mutation and recombination in real and simulated proteins with only four parameters: (i) the amino acid sequence distance between parents, (ii) the number of substitutions, (iii) the average probability that random substitutions will preserve function, and (iv) the average probability that substitutions generated by recombination will preserve function. Our results expose a fundamental functional enrichment in regions of protein sequence space accessible by recombination and provide a framework for evaluating whether the relative rates of mutation and recombination observed in nature reflect the underlying imbalance in their effects on protein function.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.