ArticleProceedings of the National Academy of Sciences of the United States of America2005
Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Crystal structure of Alzheimer's disease phospholipase D3 provides a molecular basis for understanding its normal and pathological functions.The FEBS journal · 2024Article
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- Structural and mechanistic insights into disease-associated endolysosomal exonucleases PLD3 and PLD4.Structure (London, England : 1993) · 2024Article
- Characterization of winged helix domain fusion endonucleases as N6-methyladenine-dependent type IV restriction systems.Frontiers in microbiology · 2024Article
- smFRET Detection of Cis and Trans DNA Interactions by the BfiI Restriction Endonuclease.The journal of physical chemistry. B · 2023Article
- Structural basis for broad anti-phage immunity by DISARM.Nature communications · 2022Article
- Crystal Structure of a Phospholipase D from the Plant-Associated BacteriaInternational journal of molecular sciences · 2021Article
- Mechanism of DNA cleavage by the endonuclease SauUSI: a major barrier to horizontal gene transfer and antibiotic resistance in Staphylococcus aureus.Nucleic acids research · 2021Article
- Crystal structure and DNA cleavage mechanism of the restriction DNA glycosylase R.CcoLI from Campylobacter coli.Scientific reports · 2021Article
- Distortion of double-stranded DNA structure by the binding of the restriction DNA glycosylase R.PabI.Nucleic acids research · 2020Article
- Characterization of Single Amino Acid Variations in an EDTA-Tolerating Non-specific Nuclease from the Ice-Nucleating Bacterium Pseudomonas syringae.Molecular biotechnology · 2020Article
- The crystal structure of theThe Journal of biological chemistry · 2018Article
- DISARM is a widespread bacterial defence system with broad anti-phage activities.Nature microbiology · 2018Article
- Tetrameric structure of the restriction DNA glycosylase R.PabI in complex with nonspecific double-stranded DNA.Scientific reports · 2016Article
- Crystal structure of the R-protein of the multisubunit ATP-dependent restriction endonuclease NgoAVII.Nucleic acids research · 2014Article
- DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis.Nucleic acids research · 2014Article
- The evolutionary journey of Argonaute proteins.Nature structural & molecular biology · 2014Review
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- Structural insight into the specificity of the B3 DNA-binding domains provided by the co-crystal structure of the C-terminal fragment of BfiI restriction enzyme.Nucleic acids research · 2014Article
- Cofactor analogue-induced chemical reactivation of endonuclease activity in a DNA cleavage/methylation deficient TspGWI N₄₇₃A variant in the NPPY motif.Molecular biology reports · 2014Article
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7 authors.
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Abstract
Among all restriction endonucleases known to date, BfiI is unique in cleaving DNA in the absence of metal ions. BfiI represents a different evolutionary lineage of restriction enzymes, as shown by its crystal structure at 1.9-A resolution. The protein consists of two structural domains. The N-terminal catalytic domain is similar to Nuc, an EDTA-resistant nuclease from the phospholipase D superfamily. The C-terminal DNA-binding domain of BfiI exhibits a beta-barrel-like structure very similar to the effector DNA-binding domain of the Mg(2+)-dependent restriction enzyme EcoRII and to the B3-like DNA-binding domain of plant transcription factors. BfiI presumably evolved through domain fusion of a DNA-recognition element to a nonspecific nuclease akin to Nuc and elaborated a mechanism to limit DNA cleavage to a single double-strand break near the specific recognition sequence. The crystal structure suggests that the interdomain linker may act as an autoinhibitor controlling BfiI catalytic activity in the absence of a specific DNA sequence. A psi-blast search identified a BfiI homologue in a Mesorhizobium sp. BNC1 bacteria strain, a plant symbiont isolated from an EDTA-rich environment.
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