ArticleScientific reports2014
Single molecular investigation of DNA looping and aggregation by restriction endonuclease BspMI.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structures, activity and mechanism of the Type IIS restriction endonuclease PaqCI.Nucleic acids research · 2023Article
- Molecular Recognition of Proteins through Quantitative Force Maps at Single Molecule Level.Biomolecules · 2022Article
- DNA-Lysozyme Nanoarchitectonics: Quantitative Investigation on Charge Inversion and Compaction.Polymers · 2022Article
- Demonstration of pH-controlled DNA-surfactant manipulation for biomolecules.RSC advances · 2021Article
- Bending and looping of long DNA by Polycomb repressive complex 2 revealed by AFM imaging in liquid.Nucleic acids research · 2020Article
- Investigating the Influence of Magnesium Ions on p53-DNA Binding Using Atomic Force Microscopy.International journal of molecular sciences · 2017Article
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Authors and funding
3 authors.
Funding
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Abstract
DNA looping and aggregation induced by restriction endonuclease BspMI are studied by atomic force microscopy (AFM) and magnetic tweezers (MT). With Ca(2+) substituted for the normal enzyme cofactor Mg(2+) and enzyme concentration below the critical concentration of 6 units/mL, AFM images of DNA-BspMI complex show that the number of binding and looping events increases with enzyme concentration. At the critical concentration 6 of units/mL, all the BspMI binding sites are saturated. It is worth noting that nonspecific BspMI binding to DNA at saturation concentration represents more than 8% of the total BspMI-DNA complexes directly observed in AFM images. Furthermore, we used MT to prove that additional loops can form when enzyme concentration is higher than its saturation valueand the complex is incubated for a long time (>2 hrs). We ascribe this phenomenon to the aggregation of enzymes. The force spectroscopy of the BspMI-DNA complex shows that the pulling force required to open the loop of the complex at less than saturation concentration has a peak at about 3 pN, which is lower than the force required to open additional loops due to enzyme aggregation at higher than saturation concentration (>6 pN).
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