ArticleProceedings of the National Academy of Sciences of the United States of America2006
Tension-dependent DNA cleavage by restriction endonucleases: two-site enzymes are "switched off" at low force.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 52 citations in OpenAlex.
- The ultrafine-bridge-associated endonuclease ANKLE1 is stimulated by tension in DNA to process branch-points.Nucleic acids research · 2026Article
- The interplay between supercoiling and DNA modifying enzymes at the single-molecule level.Scientific reports · 2026Article
- ANKLE1 processes chromatin bridges by cleaving mechanically stressed DNA.Nature communications · 2025Article
- Restriction endonuclease selective inhibition by β-cyclodextrin sulfate.Bioscience reports · 2025Article
- Understanding protein diffusion on force-induced stretched DNA conformation.Frontiers in molecular biosciences · 2022Article
- DNA Manipulation and Single-Molecule Imaging.Molecules (Basel, Switzerland) · 2021Review
- Novel parameter describing restriction endonucleases: Secondary-Cognate-Specificity and chemical stimulation of TsoI leading to substrate specificity change.Applied microbiology and biotechnology · 2019Article
- Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- A new direct single-molecule observation method for DNA synthesis reaction using fluorescent replication protein A.Sensors (Basel, Switzerland) · 2014Article
- DNA looping by FokI: the impact of synapse geometry on loop topology at varied site orientations.Nucleic acids research · 2012Article
- On the role of DNA biomechanics in the regulation of gene expression.Journal of the Royal Society, Interface · 2011Review
- DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion.Nucleic acids research · 2011Article
- 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
- Downstream DNA tension regulates the stability of the T7 RNA polymerase initiation complex.Biophysical journal · 2011Article
- Differences between Ca2+ and Mg2+ in DNA binding and release by the SfiI restriction endonuclease: implications for DNA looping.Nucleic acids research · 2009Article
- Creation of a type IIS restriction endonuclease with a long recognition sequence.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
- The effect of physical form of DNA on exonucleaseIII activity revealed by single-molecule observations.Journal of fluorescence · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA looping occurs in many important protein-DNA interactions, including those regulating replication, transcription, and recombination. Recent theoretical studies predict that tension of only a few piconewtons acting on DNA would almost completely inhibit DNA looping. Here, we study restriction endonucleases that require interaction at two separated sites for efficient cleavage. Using optical tweezers we measured the dependence of cleavage activity on DNA tension with 15 known or suspected two-site enzymes (BfiI, BpmI, BsgI, BspMI, Cfr9I, Cfr10I, Eco57I, EcoRII, FokI, HpaII, MboII, NarI, SacII, Sau3AI, and SgrAI) and six one-site enzymes (BamHI, EcoRI, EcoRV, HaeIII, HindIII, and DNaseI). All of the one-site enzymes were virtually unaffected by 5 pN of tension, whereas all of the two-site enzymes were completely inhibited. These enzymes thus constitute a remarkable example of a tension sensing "molecular switch." A detailed study of one enzyme, Sau3AI, indicated that the activity decreased exponentially with tension and the decrease was approximately 10-fold at 0.7 pN. At higher forces (approximately 20-40 pN) cleavage by the one-site enzymes EcoRV and HaeIII was partly inhibited and cleavage by HindIII was enhanced, whereas BamHI, EcoRI, and DNaseI were largely unaffected. These findings correlate with structural data showing that EcoRV bends DNA sharply, whereas BamHI, EcoRI, and DNaseI do not. Thus, DNA-directed enzyme activity involving either DNA looping or bending can be modulated by tension, a mechanism that could facilitate mechanosensory transduction in vivo.
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