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作 者:许会沙 周浩[1] Xu Huisha;Zhou Hao(College of Life Sciences, Nankai University, Tianjin 300071, China)
出 处:《南开大学学报(自然科学版)》2018年第2期26-30,共5页Acta Scientiarum Naturalium Universitatis Nankaiensis
基 金:国家自然科学基金(31171284)
摘 要:SWI/SNF复合体是由多个亚基组成的复合物在真核细胞中具有较高的保守性,能通过其自身ATP酶的活性调节染色质的结构,从而影响大量基因的表达,在人类神经系统的发育形成和功能发挥中起重要作用.SNF11是酵母SWI/SNF复合体中的一个亚基组分,能与核心亚基SWI2/SNF2相互作用.在本研究中,构建了p ET.32M.3C-SNF11的表达质粒,大量表达出SNF11的重组蛋白,通过Ni柱亲和层析和分子筛层析技术得到较纯的SNF11蛋白,并用分析型分子筛层析技术分析了蛋白的构象和聚集状况,为进一步研究SNF11蛋白与SWI/SNF复合体中其他亚基组分的相互作用提供了一定的基础.The SWI/SNF complex is consistent of numbers of subunits, and is very conservative in eukaryotic cells. The SWI/SNF complex can change the structure of chromatin by its ATPase activity,and then regulates the gene expression. What's more, the SWI/SNF complex plays an important role in the development and function of the nervous system in human. SNF11 is one of the subunits of the SWI/SNF complex. In the research, we constructed the plasmid of p ET.32 M.3 C-SNF11, expressed the recombinant protein TRX-SNF11, and purified SNF11 through Ni-affinity chromatography and size exclusion chromatography. More, we analysis the conformation and aggregation of SNF11 by analytical size exclusion chromatography. Collectively, our observations may provide a base for further study of the interaction between SNF11 and other subunits of SWI/SNF complex.
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