ArticleNucleic acids research2006
RAISE: a simple and novel method of generating random insertion and deletion mutations.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 55 citations in OpenAlex.
- High-throughput methods enabling random duplications, deletions, or nucleotide-constrained mutagenesis of entire DNA motifs.Nucleic acids research · 2026Article
- Combing Directed Enzyme Evolution with Metabolic Engineering to Develop Efficient Microbial Cell Factories.Chem & bio engineering · 2025Review
- Automated Engineering Protein Dynamics via Loop Grafting: ImprovingACS catalysis · 2025Article
- In vitro generation of genetic diversity for directed evolution by error-prone artificial DNA synthesis.Communications biology · 2024Article
- A primer to directed evolution: current methodologies and future directions.RSC chemical biology · 2023Review
- A novel framework for engineering protein loops exploring length and compositional variation.Scientific reports · 2021Article
- Gene-specific mutagenesis enables rapid continuous evolution of enzymes in vivo.Nucleic acids research · 2021Article
- Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity.The Journal of biological chemistry · 2020Article
- Improvement of Lead Tolerance of Saccharomyces cerevisiae by Random Mutagenesis of Transcription Regulator SPT3.Applied biochemistry and biotechnology · 2018Article
- Extensive libraries of gene truncation variants generated by in vitro transposition.Nucleic acids research · 2017Article
- Structural plasticity of green fluorescent protein to amino acid deletions and fluorescence rescue by folding-enhancing mutations.BMC biochemistry · 2015Article
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Structural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent protein.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Random single amino acid deletion sampling unveils structural tolerance and the benefits of helical registry shift on GFP folding and structure.Structure (London, England : 1993) · 2014Article
- Microbial enzymes: tools for biotechnological processes.Biomolecules · 2014Review
- Network models of TEM β-lactamase mutations coevolving under antibiotic selection show modular structure and anticipate evolutionary trajectories.PLoS computational biology · 2011Article
- Exploring protein fitness landscapes by directed evolution.Nature reviews. Molecular cell biology · 2009Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although proteins may be artificially improved by random insertion and deletion mutagenesis methods, these procedures are technically difficult, and the mutations introduced are no more variable than those introduced by the introduction of random point mutations. We describe here a three-step method called RAISE, which is based on gene shuffling and can introduce a wide variety of insertions, deletions and substitutions. To test the efficacy of this method, we used it to mutate TEM beta-lactamase to generate improved antibiotic resistance. Some unique insertion or deletion mutations were observed in the improved mutants, some of which caused higher activities than point mutations. Our findings indicate that the RAISE method can yield unique mutants and may be a powerful technique of protein engineering.
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