ArticleNucleic acids research2007
The C-terminal loop of the homing endonuclease I-CreI is essential for site recognition, DNA binding and cleavage.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Targeted mutagenesis with sequence-specific nucleases for accelerated improvement of polyploid crops: Progress, challenges, and prospects.The plant genome · 2023Review
- Improvements of nuclease and nickase gene modification techniques for the treatment of genetic diseases.Frontiers in genome editing · 2022Review
- Modern Trends in Plant Genome Editing: An Inclusive Review of the CRISPR/Cas9 Toolbox.International journal of molecular sciences · 2019Review
- Understanding the indirect DNA read-out specificity of I-CreI Meganuclease.Scientific reports · 2018Article
- The Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease.Journal of molecular biology · 2016Article
- Engineering a Nickase on the Homing Endonuclease I-DmoI Scaffold.The Journal of biological chemistry · 2015Article
- Advanced genetic tools for plant biotechnology.Nature reviews. Genetics · 2013Review
- Non-specific protein-DNA interactions control I-CreI target binding and cleavage.Nucleic acids research · 2012Article
- Meganucleases and other tools for targeted genome engineering: perspectives and challenges for gene therapy.Current gene therapy · 2011Review
- Molecular basis of engineered meganuclease targeting of the endogenous human RAG1 locus.Nucleic acids research · 2011Article
- Generation of redesigned homing endonucleases comprising DNA-binding domains derived from two different scaffolds.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Meganucleases are sequence-specific endonucleases with large cleavage sites that can be used to induce efficient homologous gene targeting in cultured cells and plants. These enzymes open novel perspectives for genome engineering in a wide range of fields, including gene therapy. A new crystal structure of the I-CreI dimer without DNA has allowed the comparison with the DNA-bound protein. The C-terminal loop displays a different conformation, which suggests its implication in DNA binding. A site-directed mutagenesis study in this region demonstrates that whereas the C-terminal helix is negligible for DNA binding, the final C-terminal loop is essential in DNA binding and cleavage. We have identified two regions that comprise the Ser138-Lys139 and Lys142-Thr143 pairs whose double mutation affect DNA binding in vitro and abolish cleavage in vivo. However, the mutation of only one residue in these sites allows DNA binding in vitro and cleavage in vivo. These findings demonstrate that the C-terminal loop of I-CreI endonuclease plays a fundamental role in its catalytic mechanism and suggest this novel site as a region to take into account for engineering new endonucleases with tailored specificity.
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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.