ArticleNucleic acids research2010
DNA synapsis through transient tetramerization triggers cleavage by Ecl18kI restriction enzyme.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- Unique mechanism of target recognition by PfoI restriction endonuclease of the CCGG-family.Nucleic acids research · 2019Article
- Structure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI.Nucleic acids research · 2019Article
- A-ZIP53, a dominant negative reveals the molecular mechanism of heterodimerization between bZIP53, bZIP10 and bZIP25 involved in Arabidopsis seed maturation.Scientific reports · 2017Article
- UbaLAI is a monomeric Type IIE restriction enzyme.Nucleic acids research · 2017Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA.Nucleic acids research · 2017Article
- DNA-Endonuclease Complex Dynamics by Simultaneous FRET and Fluorophore Intensity in Evanescent Field.Biophysical journal · 2017Article
- Lifespan of restriction-modification systems critically affects avoidance of their recognition sites in host genomes.BMC genomics · 2015Article
- Functional significance of protein assemblies predicted by the crystal structure of the restriction endonuclease BsaWI.Nucleic acids research · 2015Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- MADS domain transcription factors mediate short-range DNA looping that is essential for target gene expression in Arabidopsis.The Plant cell · 2013Article
- Restriction endonuclease TseI cleaves A:A and T:T mismatches in CAG and CTG repeats.Nucleic acids research · 2013Article
- Organization of the BcgI restriction-modification protein for the cleavage of eight phosphodiester bonds in DNA.Nucleic acids research · 2013Article
- Structure and cleavage activity of the tetrameric MspJI DNA modification-dependent restriction endonuclease.Nucleic acids research · 2012Article
- High-throughput single-molecule analysis of DNA-protein interactions by tethered particle motion.Nucleic acids research · 2012Article
- DNA looping by FokI: the impact of synapse geometry on loop topology at varied site orientations.Nucleic acids research · 2012Article
- DNA looping by FokI: the impact of twisting and bending rigidity on protein-induced looping dynamics.Nucleic acids research · 2012Article
- Concerted action at eight phosphodiester bonds by the BcgI restriction endonuclease.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
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
To cut DNA at their target sites, restriction enzymes assemble into different oligomeric structures. The Ecl18kI endonuclease in the crystal is arranged as a tetramer made of two dimers each bound to a DNA copy. However, free in solution Ecl18kI is a dimer. To find out whether the Ecl18kI dimer or tetramer represents the functionally important assembly, we generated mutants aimed at disrupting the putative dimer-dimer interface and analysed the functional properties of Ecl18kI and mutant variants. We show by atomic force microscopy that on two-site DNA, Ecl18kI loops out an intervening DNA fragment and forms a tetramer. Using the tethered particle motion technique, we demonstrate that in solution DNA looping is highly dynamic and involves a transient interaction between the two DNA-bound dimers. Furthermore, we show that Ecl18kI cleaves DNA in the synaptic complex much faster than when acting on a single recognition site. Contrary to Ecl18kI, the tetramerization interface mutant R174A binds DNA as a dimer, shows no DNA looping and is virtually inactive. We conclude that Ecl18kI follows the association model for the synaptic complex assembly in which it binds to the target site as a dimer and then associates into a transient tetrameric form to accomplish the cleavage reaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.