ArticleNucleic acids research2004
Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Short-range translocation by a restriction enzyme motor triggers diffusion along DNA.Nature chemical biology · 2024Article
- 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
- Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes.Nucleic acids research · 2015Article
- Type III restriction-modification enzymes: a historical perspective.Nucleic acids research · 2014Review
- 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
- 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
- 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
- Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases.Biochemical Society transactions · 2011Review
- Conflicts targeting epigenetic systems and their resolution by cell death: novel concepts for methyl-specific and other restriction systems.DNA research : an international journal for rapid publication of reports on genes and genomes · 2010Review
- Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Maintaining a sense of direction during long-range communication on DNA.Biochemical Society transactions · 2010Review
- The single polypeptide restriction-modification enzyme LlaGI is a self-contained molecular motor that translocates DNA loops.Nucleic acids research · 2009Article
- S-adenosyl homocysteine and DNA ends stimulate promiscuous nuclease activities in the Type III restriction endonuclease EcoPI.Nucleic acids research · 2009Article
- Type III restriction enzymes communicate in 1D without looping between their target sites.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- MmeI: a minimal Type II restriction-modification system that only modifies one DNA strand for host protection.Nucleic acids research · 2008Article
- DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes.The EMBO journal · 2007Article
- Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Characterization of the Type III restriction endonuclease PstII from Providencia stuartii.Nucleic acids research · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type III restriction enzymes have been demonstrated to require two unmethylated asymmetric recognition sites oriented head-to-head to elicit double-strand break 25-27 bp downstream of one of the two sites. The proposed DNA cleavage mechanism involves ATP-dependent DNA translocation. The sequence context of the recognition site was suggested to influence the site of DNA cleavage by the enzyme. In this investigation, we demonstrate that the cleavage site of the R.EcoP15I restriction enzyme does not depend on the sequence context of the recognition site. Strikingly, this study demonstrates that the enzyme can cleave linear DNA having either recognition sites in the same orientation or a single recognition site. Cleavage occurs predominantly at a site proximal to the DNA end in the case of multiple site substrates. Such cleavage can be abolished by the binding of Lac repressor downstream (3' side) but not upstream (5' side) of the recognition site. Binding of HU protein has also been observed to interfere with R.EcoP15I cleavage activity. In accordance with a mechanism requiring two enzyme molecules cooperating to elicit double-strand break on DNA, our results convincingly demonstrate that the enzyme translocates on DNA in a 5' to 3' direction from its recognition site and indicate a switch in the direction of enzyme motion at the DNA ends. This study demonstrates a new facet in the mode of action of these restriction enzymes.
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