ArticleNucleic acids research2007
Catalytic domain of restriction endonuclease BmrI as a cleavage module for engineering endonucleases with novel substrate specificities.
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, 25 citations in OpenAlex.
- Modular determinants of cleavage preference in GIY-YIG nucleases revealed by block-based DNA shuffling and directed evolution.Nucleic acids research · 2026Article
- Characterization of winged helix domain fusion endonucleases as N6-methyladenine-dependent type IV restriction systems.Frontiers in microbiology · 2024Article
- An alternative novel tool for DNA editing without target sequence limitation: the structure-guided nuclease.Genome biology · 2016Article
- Generation of artificial sequence-specific nucleasesChemical science · 2016Article
- Creating highly specific nucleases by fusion of active restriction endonucleases and catalytically inactive homing endonucleases.Nucleic acids research · 2012Article
- Characterization of type II and III restriction-modification systems from Bacillus cereus strains ATCC 10987 and ATCC 14579.Journal of bacteriology · 2012Article
- Creation of a novel telomere-cutting endonuclease based on the EN domain of telomere-specific non-long terminal repeat retrotransposon, TRAS1.Mobile DNA · 2010Article
- Creation of a type IIS restriction endonuclease with a long recognition sequence.Nucleic acids research · 2009Article
- Evolution of sequence specificity in a restriction endonuclease by a point mutation.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Template-directed addition of nucleosides to DNA by the BfiI restriction enzyme.Nucleic acids research · 2008Article
- Tetrameric restriction enzymes: expansion to the GIY-YIG nuclease family.Nucleic acids research · 2008Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Creating endonucleases with novel sequence specificities provides more possibilities to manipulate DNA. We have created a chimeric endonuclease (CH-endonuclease) consisting of the DNA cleavage domain of BmrI restriction endonuclease and C.BclI, a controller protein of the BclI restriction-modification system. The purified chimeric endonuclease, BmrI198-C.BclI, cleaves DNA at specific sites in the vicinity of the recognition sequence of C.BclI. Double-strand (ds) breaks were observed at two sites: 8 bp upstream and 18 bp within the C-box sequence. Using DNA substrates with deletions of C-box sequence, we show that the chimeric endonuclease requires the 5' half of the C box only for specific cleavage. A schematic model is proposed for the mode of protein-DNA binding and DNA cleavage. The present study demonstrates that the BmrI cleavage domain can be used to create combinatorial endonucleases that cleave DNA at specific sequences dictated by the DNA-binding partner. The resulting endonucleases will be useful in vitro and in vivo to create ds breaks at specific sites and generate deletions.
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Registered trials
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.