ArticleProceedings of the National Academy of Sciences of the United States of America2008
Crystal structure of I-DmoI in complex with its target DNA provides new insights into meganuclease engineering.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Can Designer Indels Be Tailored by Gene Editing?: Can Indels Be Customized?BioEssays : news and reviews in molecular, cellular and developmental biology · 2019Article
- Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI.Journal of computer-aided molecular design · 2017Article
- Structure of the I-SceI nuclease complexed with its dsDNA target and three catalytic metal ions.Acta crystallographica. Section F, Structural biology communications · 2016Article
- The Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease.Journal of molecular biology · 2016Article
- Crystal Structure of the Homing Endonuclease I-CvuI Provides a New Template for Genome Modification.The Journal of biological chemistry · 2015Article
- Engineering a Nickase on the Homing Endonuclease I-DmoI Scaffold.The Journal of biological chemistry · 2015Article
- Fast and sensitive detection of indels induced by precise gene targeting.Nucleic acids research · 2015Article
- Visualizing phosphodiester-bond hydrolysis by an endonuclease.Nature structural & molecular biology · 2015Article
- Massively parallel determination and modeling of endonuclease substrate specificity.Nucleic acids research · 2014Article
- Non-specific protein-DNA interactions control I-CreI target binding and cleavage.Nucleic acids research · 2012Article
- Manipulating piggyBac transposon chromosomal integration site selection in human cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2011Article
- Context dependence between subdomains in the DNA binding interface of the I-CreI homing endonuclease.Nucleic acids research · 2011Article
- Meganucleases and other tools for targeted genome engineering: perspectives and challenges for gene therapy.Current gene therapy · 2011Review
- Using protein design algorithms to understand the molecular basis of disease caused by protein-DNA interactions: the Pax6 example.Nucleic acids research · 2010Article
- Generation of redesigned homing endonucleases comprising DNA-binding domains derived from two different scaffolds.Nucleic acids research · 2010Article
- Homing endonucleases: from basics to therapeutic applications.Cellular and molecular life sciences : CMLS · 2010Review
- Efficient targeting of a SCID gene by an engineered single-chain homing endonuclease.Nucleic acids research · 2009Article
- Motif-directed flexible backbone design of functional interactions.Protein science : a publication of the Protein Society · 2009Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homing endonucleases, also known as meganucleases, are sequence-specific enzymes with large DNA recognition sites. These enzymes can be used to induce efficient homologous gene targeting in cells and plants, opening perspectives for genome engineering with applications in a wide series of fields, ranging from biotechnology to gene therapy. Here, we report the crystal structures at 2.0 and 2.1 A resolution of the I-DmoI meganuclease in complex with its substrate DNA before and after cleavage, providing snapshots of the catalytic process. Our study suggests that I-DmoI requires only 2 cations instead of 3 for DNA cleavage. The structure sheds light onto the basis of DNA binding, indicating key residues responsible for nonpalindromic target DNA recognition. In silico and in vivo analysis of the I-DmoI DNA cleavage specificity suggests that despite the relatively few protein-base contacts, I-DmoI is highly specific when compared with other meganucleases. Our data open the door toward the generation of custom endonucleases for targeted genome engineering using the monomeric I-DmoI scaffold.
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