ArticleThe EMBO journal1997
Mapping metal ions at the catalytic centres of two intron-encoded endonucleases.
Article in The EMBO journal, 1997. 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, 37 citations in OpenAlex.
- Recent Insights Into the Structure, Function, and Evolution of the RNA-Splicing Endonucleases.Frontiers in genetics · 2019Review
- Engineering a Nickase on the Homing Endonuclease I-DmoI Scaffold.The Journal of biological chemistry · 2015Article
- Mutational analysis of active-site residues in the Mycobacterium leprae RecA intein, a LAGLIDADG homing endonuclease: Asp(122) and Asp(193) are crucial to the double-stranded DNA cleavage activity whereas Asp(218) is not.Protein science : a publication of the Protein Society · 2010Article
- Biochemical and mutagenic analysis of I-CreII reveals distinct but important roles for both the H-N-H and GIY-YIG motifs.Nucleic acids research · 2009Article
- Crystal structure of I-DmoI in complex with its target DNA provides new insights into meganuclease engineering.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Engineering variants of the I-SceI homing endonuclease with strand-specific and site-specific DNA-nicking activity.Journal of molecular biology · 2008Article
- Mutational analysis of highly conserved aspartate residues essential to the catalytic core of the piggyBac transposase.BMC molecular biology · 2008Article
- A novel engineered meganuclease induces homologous recombination in yeast and mammalian cells.Nucleic acids research · 2003Article
- The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif.The EMBO journal · 2002Article
- Homing endonucleases: structural and functional insight into the catalysts of intron/intein mobility.Nucleic acids research · 2001Review
- Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase.Genes & development · 1999Article
- An unspliced group I intron in 23S rRNA links Chlamydiales, chloroplasts, and mitochondria.Journal of bacteriology · 1999Article
- Detection of RAG protein-V(D)J recombination signal interactions near the site of DNA cleavage by UV cross-linking.Molecular and cellular biology · 1999Article
- The protein splicing domain of the homing endonuclease PI-sceI is responsible for specific DNA binding.Nucleic acids research · 1998Article
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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
Divalent metal ions play a crucial role in forming the catalytic centres of DNA endonucleases. Substitution of Mg2+ ions by Fe2+ ions in two archaeal intron-encoded homing endonucleases, I-DmoI and I-PorI, yielded functional enzymes and enabled the generation of reactive hydroxyl radicals within the metal ion binding sites. Specific hydroxyl radical-induced cleavage was observed within, and immediately after, two conserved LAGLIDADG motifs in both proteins and at sites at, and near, the scissile phosphates of the corresponding DNA substrates. Titration of Fe2+-containing protein-DNA complexes with Ca2+ ions, which are unable to support endonucleolytic activity, was performed to distinguish between the individual metal ions in the complex. Mutations of single amino acids in this region impaired catalytic activity and caused the preferential loss of a subset of hydroxyl radical cleavages in both the protein and the DNA substrate, suggesting an active role in metal ion coordination for these amino acids. The data indicate that the endonucleases cleave their DNA substrates as monomeric enzymes, and contain a minimum of four divalent metal ions located at or near the catalytic centres of each endonuclease. The metal ions involved in cleaving the coding and the non-coding strand are positioned immediately after the N- and C-terminally located LAGLIDADG motifs, respectively. The dual protein/nucleic acid footprinting approach described here is generally applicable to other protein-nucleic acid complexes when the natural metal ion can be replaced by Fe2+.
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