Probing the mechanical stability of bridged DNA-H-NS protein complexes by single-molecule AFM pulling
文献类型： 外文期刊
作者： Liang, Yan 1 ; van der Valk, Ramon A. 5 ; Dame, Remus T. 3 ; Roos, Wouter H. 3 ; Wuite, Gijs J. L. 3 ;
作者机构： 1.Chinese Acad Fishery Sci, Qingdao Natl Lab Marine Sci & Technol, Funct Lab Marine Fisheries Sci & Food Prod Proc, Qingdao, Peoples R China
2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao, Peoples R China
3.Vrije Univ Amsterdam, Dept Phys & Astron, Amsterdam, Netherlands
4.Vrije Univ Amsterdam, LaserLab, Amsterdam, Netherlands
5.Leiden Univ, Leiden Inst Chem & Cell Observ, Leiden, Netherlands
6.Univ Groningen, Zernike Inst, Mol Biofys, Groningen, Netherlands
期刊名称：SCIENTIFIC REPORTS （ 影响因子：4.379； 五年影响因子：5.133 ）
ISSN： 2045-2322
年卷期： 2017 年 7 卷
页码：
收录情况： SCI
摘要： Atomic force microscopy (AFM) has proven to be a powerful tool for the study of DNA-protein interactions due to its ability to image single molecules at the nanoscale. However, the use of AFM in force spectroscopy to study DNA-protein interactions has been limited. Here we developed a high throughput, AFM based, pulling assay to measure the strength and kinetics of protein bridging of DNA molecules. As a model system, we investigated the interactions between DNA and the Histone-like Nucleoid-Structuring protein (H-NS). We confirmed that H-NS both changes DNA rigidity and forms bridges between DNA molecules. This straightforward methodology provides a high-throughput approach with single-molecule resolution which is widely applicable to study cross-substrate interactions such as DNA-bridging proteins.
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