中文题名: | 锌指蛋白ZNF830与PPIL2复合物及其晶体的初步探究 |
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保密级别: | 公开 |
论文语种: | 中文 |
学科代码: | 070301 |
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学生类型: | 学士 |
学位: | 理学学士 |
学位年度: | 2019 |
学校: | 北京师范大学 |
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提交日期: | 2019-05-20 |
答辩日期: | 2019-05-22 |
中文关键词: | 锌指蛋白ZNF830 ; PPIL2 ; DNA同源重组修复 ; 蛋白质相互作用 ; 锌指蛋白ZNF830 ; PPIL2复合物 |
中文摘要: |
DNA损伤在人们的日常生活中持续发生,对基因组的稳定性具有极大的威胁,容易造成各种疾病。因此,DNA修复对于维持基因组的稳定具有重要的意义。有研究结果表明,锌指蛋白ZNF830能够促进DNA同源重组修复(HR)。在实验室的前期工作中发现,泛素连接酶PPIL2与ZNF830存在相互作用。本课题通过GST-Pulldown实验探究锌指蛋白ZNF830的C端和泛素连接酶PPIL2的C端为主要相互作用区域。并通过在大肠杆菌中共转化的方式得到了ZNF830与PPIL2全长/C端的复合物,并且尝试获得复合物晶体。本课题为确定ZNF830在生物细胞内生理过程提供理论依据和方向,为研究治疗癌症的药物提供新的可能。
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外文摘要: |
DNA damage continues to occur in people's daily lives, and it poses a great threat to the stability of the genome and is prone to various diseases. Therefore, DNA repair is important for maintaining the stability of the genome. Studies have shown that zinc finger protein ZNF830 can promote DNA homologous recombination repair (HR). In the preliminary work of the laboratory, it was found that the ubiquitin ligase PPIL2 interacts with ZNF830. In this study, the C-terminus of zinc finger protein ZNF830 and the C-terminus of ubiquitin ligase PPIL2 were explored as the main interaction regions by GST-Pulldown assay. A complex of ZNF830 and PPIL2 full-length/C-terminus was obtained by co-transformation in E. coli, and an attempt was made to obtain a complex crystal. This topic provides a theoretical basis and direction for determining the physiological processes of ZNF830 in biological cells, and provides new possibilities for studying drugs for treating cancer.
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参考文献总数: | 27 |
插图总数: | 10 |
插表总数: | 3 |
馆藏号: | 本070301/19012 |
开放日期: | 2020-07-09 |