Interaction Study between DNA and Histone Proteins on Single-molecule Level using Atomic Force Microscopy  

利用原子力显微镜研究在单分子水平上DNA与组蛋白的相互作用

作　　者：刘玉颖[1] 王鹏业[2] 窦硕星[2] 吕洪凤[1] 

机构地区：[1]中国农业大学理学院,北京100083 [2]中国科学院物理研究所软物质物理实验室,北京100190

出　　处：《Chinese Journal of Chemical Physics》2014年第1期115-120,I0004,共7页化学物理学报（英文）

基　　金：ACKNOWLEDGMENTS This work was supported by the National Natural Science Foundation of China （No.11274374）, the National Basic Research Program of China （No.2009CB930704）, and the Basic Scientific Research Foundation of China Agricultural University （No.2012QJ026）.

摘　　要：DNA and histone protein are important in the formation of nucleosomal arrays, which are the first packaging level of DNA into a more compact chromatin structure. To characterize the interactions of DNA and histone proteins, we reconstitute nucleosomes using lambda DNA and whole histone proteins by dialysis and perform direct atomic force microscopy （AFM） imaging. Compared with non-specific DNA and histone binding, nucleosomes are formed within the assembled “beads-on-a-string” nucleosomal array by dialysis. These observations facilitate the establishment of the molecular mechanisms of nucleosome and demonstrate the capability of AFM for protein-DNA interaction analysis.

关 键 词：DNA HISTONE Atomic force microscopy Single molecule DIALYSIS 

分 类 号：O6[理学—化学]