ArticleThe EMBO journal2000
Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 113 citations in OpenAlex.
- Structural and functional investigation of GajB protein in Gabija anti-phage defense.Nucleic acids research · 2023Article
- A Gel-Based Assay for Probing Protein Translocation on dsDNA.Bio-protocol · 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
- DNA-mediated coupling of ATPase, translocase and nuclease activities of a Type ISP restriction-modification enzyme.Nucleic acids research · 2020Article
- RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions.Nature communications · 2018Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation.PeerJ · 2017Article
- Double-stranded DNA translocase activity of transcription factor TFIIH and the mechanism of RNA polymerase II open complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.PloS one · 2015Article
- Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.Nature communications · 2014Article
- Analysis of the activities of RAD54, a SWI2/SNF2 protein, using a specific small-molecule inhibitor.The Journal of biological chemistry · 2013Article
- Superfamily 2 helicases.Frontiers in bioscience (Landmark edition) · 2012Review
- Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex.Nucleic acids research · 2012Article
- Structural and functional analysis of the symmetrical Type I restriction endonuclease R.EcoR124IPloS one · 2012Article
- Fluorescence methods to study DNA translocation and unwinding kinetics by nucleic acid motors.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Recycling of protein subunits during DNA translocation and cleavage by Type I restriction-modification enzymes.Nucleic acids research · 2011Article
- Efficient preparation of internally modified single-molecule constructs using nicking enzymes.Nucleic acids research · 2011Article
- 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
- Sequence-specific assembly of FtsK hexamers establishes directional translocation on DNA.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- 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
Corrections and comments
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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
The type I restriction enzyme EcoR124I cleaves DNA following extensive linear translocation dependent upon ATP hydrolysis. Using protein-directed displacement of a DNA triplex, we have determined the kinetics of one-dimensional motion without the necessity of measuring DNA or ATP hydrolysis. The triplex was pre-formed specifically on linear DNA, 4370 bp from an EcoR124I site, and then incubated with endonuclease. Upon ATP addition, a distinct lag phase was observed before the triplex-forming oligonucleotide was displaced with exponential kinetics. As the distance between type I and triplex sites was shortened, the lag time decreased whilst the displacement reaction remained exponential. This is indicative of processive DNA translocation followed by collision with the triplex and oligonucleotide displacement. A linear relationship between lag duration and inter-site distance gives a translocation velocity of 400+/-32 bp/s at 20 degrees C. Furthermore, the data can only be explained by bi-directional translocation. An endonuclease with only one of the two HsdR subunits responsible for motion could still catalyse translocation. The reaction is less processive, but can 'reset' in either direction whenever the DNA is released.
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