ArticleNucleic acids research2017
Crystallographic analyses illustrate significant plasticity and efficient recoding of meganuclease target specificity.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The activity, divergence, and evolutionary degradation of modern-day homing endonucleases and behavior of their reconstructed ancestors.Nucleic acids research · 2026Article
- Review
- Caveat emptor: predicting and modeling protein-DNA recognition and binding via machine-learning computational approaches.Nucleic acids research · 2026Review
- RESET: A TCR-coupled antigen receptor with superior targeting sensitivity and reversible drug-regulated anti-tumor activity.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Review
- Article
- I-SceI and customized meganucleases-mediated genome editing in tomato and oilseed rape.Transgenic research · 2022Article
- Gene Editing in Pluripotent Stem Cells and Their Derived Organoids.Stem cells international · 2021Review
- Optimization of Protein Thermostability and Exploitation of Recognition Behavior to Engineer Altered Protein-DNA Recognition.Structure (London, England : 1993) · 2020Article
- 'Off-the-shelf' allogeneic CAR T cells: development and challenges.Nature reviews. Drug discovery · 2020Review
- Modifying a covarying protein-DNA interaction changes substrate preference of a site-specific endonuclease.Nucleic acids research · 2019Article
- Engineering altered protein-DNA recognition specificity.Nucleic acids research · 2018Review
- Gene drives to fight malaria: current state and future directions.Pathogens and global health · 2017Review
- Tuning DNA binding affinity and cleavage specificity of an engineered gene-targeting nuclease via surface display, flow cytometry and cellular analyses.Protein engineering, design & selection : PEDS · 2017Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The retargeting of protein-DNA specificity, outside of extremely modular DNA binding proteins such as TAL effectors, has generally proved to be quite challenging. Here, we describe structural analyses of five different extensively retargeted variants of a single homing endonuclease, that have been shown to function efficiently in ex vivo and in vivo applications. The redesigned proteins harbor mutations at up to 53 residues (18%) of their amino acid sequence, primarily distributed across the DNA binding surface, making them among the most significantly reengineered ligand-binding proteins to date. Specificity is derived from the combined contributions of DNA-contacting residues and of neighboring residues that influence local structural organization. Changes in specificity are facilitated by the ability of all those residues to readily exchange both form and function. The fidelity of recognition is not precisely correlated with the fraction or total number of residues in the protein-DNA interface that are actually involved in DNA contacts, including directional hydrogen bonds. The plasticity of the DNA-recognition surface of this protein, which allows substantial retargeting of recognition specificity without requiring significant alteration of the surrounding protein architecture, reflects the ability of the corresponding genetic elements to maintain mobility and persistence in the face of genetic drift within potential host target sites.
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