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首页> 外文期刊>Biochemistry >Single-Molecule Dynamics of the DNA−EcoRII Protein Complexes Revealed with High-Speed Atomic Force Microscopy
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Single-Molecule Dynamics of the DNA−EcoRII Protein Complexes Revealed with High-Speed Atomic Force Microscopy

机译：DNA-EcoRII蛋白复合物的单分子动力学与高速原子力显微镜揭示。

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摘要

The study of interactions of protein with DNA is important for gaining a fundamental understanding of how numerous biological processes occur, including recombination, transcription, repair, etc. In this study, we use the EcoRII restriction enzyme, which employs a three-site binding mechanism to catalyze cleavage of a single recognition site. Using high-speed atomic force microscopy (HS-AFM) to image single-molecule interactions in real time, we were able to observe binding, translocation, and dissociation mechanisms of the EcoRII protein. The results show that the protein can translocate along DNA to search for the specific binding site. Also, once specifically bound at a single site, the protein is capable of translocating along the DNA to locate the second specific binding site. Furthermore, two alternative modes of dissociation of the EcoRII protein from the loop structure were observed, which result in the protein stably bound as monomers to two sites or bound to a single site as a dimer. From these observations, we propose a model in which this pathway is involved in the formation and dynamics of a catalytically active three-site complex
机译：蛋白质与DNA相互作用的研究对于基本了解如何发生许多生物过程（包括重组，转录，修复等）非常重要。在这项研究中，我们使用了EcoRII限制酶，该酶采用了三位点结合机制催化单个识别位点的切割。使用高速原子力显微镜（HS-AFM）实时成像单分子相互作用，我们能够观察到EcoRII蛋白的结合，易位和解离机制。结果表明该蛋白可以沿着DNA转运以寻找特异性结合位点。而且，一旦在单个位点上特异性结合，该蛋白质就能够沿着DNA移位以定位第二个特异性结合位点。此外，观察到EcoRII蛋白从环结构解离的两种替代模式，这导致该蛋白作为单体稳定地结合至两个位点或作为二聚体结合至单个位点。从这些观察结果，我们提出了一个模型，其中该途径参与了催化活性的三部位复合物的形成和动力学。

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