ArticleProceedings of the National Academy of Sciences of the United States of America2010
Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- From CRISPR-Cas to Argonautes: Defense systems of bacteria and archaea in the hydrothermal deep subsurface.ISME communications · 2026Article
- Various plasmid strategies limit the effect of bacterial restriction-modification systems against conjugation.Nucleic acids research · 2024Article
- Short-range translocation by a restriction enzyme motor triggers diffusion along DNA.Nature chemical biology · 2024Article
- ENDO-Pore: high-throughput linked-end mapping of single DNA cleavage events using nanopore sequencing.Nucleic acids research · 2021Article
- Improving Mobilization of Foreign DNA into Zymomonas mobilis Strain ZM4 by Removal of Multiple Restriction Systems.Applied and environmental microbiology · 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
- Article
- BREX system of Escherichia coli distinguishes self from non-self by methylation of a specific DNA site.Nucleic acids research · 2019Article
- Single molecule high-throughput footprinting of small and large DNA ligands.Nature communications · 2017Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- The dynamics of the monomeric restriction endonuclease BcnI during its interaction with DNA.Nucleic acids research · 2017Article
- Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes.Nucleic acids research · 2015Article
- Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I.Nature communications · 2015Article
- Extending the range for force calibration in magnetic tweezers.Biophysical journal · 2015Article
- DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis.Nucleic acids research · 2014Article
- ClpXP protease targets long-lived DNA translocation states of a helicase-like motor to cause restriction alleviation.Nucleic acids research · 2014Article
- Type III restriction endonucleases are heterotrimeric: comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA.Nucleic acids research · 2014Article
- Type III restriction-modification enzymes: a historical perspective.Nucleic acids research · 2014Review
- The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA.Science (New York, N.Y.) · 2013Article
- DNA target sequence identification mechanism for dimer-active protein complexes.Nucleic acids research · 2013Article
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6 authors.
Funding
Abstract
Cleavage of viral DNA by the bacterial Type III Restriction-Modification enzymes requires the ATP-dependent long-range communication between a distant pair of DNA recognition sequences. The classical view is that Type III endonuclease activity is only activated by a pair of asymmetric sites in a specific head-to-head inverted repeat. Based on this assumption and due to the presence of helicase domains in Type III enzymes, various motor-driven DNA translocation models for communication have been suggested. Using both single-molecule and ensemble assays we demonstrate that Type III enzymes can also cleave DNA with sites in tail-to-tail repeat with high efficiency. The ability to distinguish both inverted repeat substrates from direct repeat substrates in a manner independent of DNA topology or accessory proteins can only be reconciled with an alternative sliding mode of communication.
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