ArticleThe EMBO journal2007
DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Short-range translocation by a restriction enzyme motor triggers diffusion along DNA.Nature chemical biology · 2024Article
- DNA-mediated coupling of ATPase, translocase and nuclease activities of a Type ISP restriction-modification enzyme.Nucleic acids research · 2020Article
- A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes.Nucleic acids research · 2018Article
- Single-site DNA cleavage by Type III restriction endonuclease requires a site-bound enzyme and a trans-acting enzyme that are ATPase-activated.Nucleic acids research · 2018Article
- Accurate nanoscale flexibility measurement of DNA and DNA-protein complexes by atomic force microscopy in liquid.Nanoscale · 2017Article
- Single-molecule studies of high-mobility group B architectural DNA bending proteins.Biophysical reviews · 2017Review
- 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
- DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin.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
- Highlights of the DNA cutters: a short history of the restriction enzymes.Nucleic acids research · 2014Article
- The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA.Science (New York, N.Y.) · 2013Article
- Dissociation from DNA of Type III Restriction-Modification enzymes during helicase-dependent motion and following endonuclease activity.Nucleic acids research · 2012Article
- Structural insights into the assembly and shape of Type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering.Journal of molecular biology · 2012Article
- Single-stranded loops as end-label polarity markers for double-stranded linear DNA templates in atomic force microscopy.Nucleic acids research · 2012Article
- Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity.Nucleic acids research · 2012Article
- DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion.Nucleic acids research · 2011Article
- Atomic force microscopy captures MutS tetramers initiating DNA mismatch repair.The EMBO journal · 2011Article
- DNA translocation by type III restriction enzymes: a comparison of current models of their operation derived from ensemble and single-molecule measurements.Nucleic acids research · 2011Review
Corrections and comments
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6 authors.
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Abstract
EcoP15I is a type III restriction enzyme that requires two recognition sites in a defined orientation separated by up to 3.5 kbp to efficiently cleave DNA. The mechanism through which site-bound EcoP15I enzymes communicate between the two sites is unclear. Here, we use atomic force microscopy to study EcoP15I-DNA pre-cleavage complexes. From the number and size distribution of loops formed, we conclude that the loops observed do not result from translocation, but are instead formed by a contact between site-bound EcoP15I and a nonspecific region of DNA. This conclusion is confirmed by a theoretical polymer model. It is further shown that translocation must play some role, because when translocation is blocked by a Lac repressor protein, DNA cleavage is similarly blocked. On the basis of these results, we present a model for restriction by type III restriction enzymes and highlight the similarities between this and other classes of restriction enzymes.
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