兰州大学机构库 >生命科学学院
AtTRN1底物的NLS分析
Alternative TitleNLS analysising of AtTRN1’ cargos
王小宁
Thesis Advisor刘恒
2015-05-29
Degree Grantor兰州大学
Place of Conferral兰州
Degree Name硕士
Keyword核质转运 AtTRN1 底物 核定位信号
Abstract目前在哺乳动物中入核转运蛋白研究较为清楚的有两大种,即Kapβ1和Kapβ2,这两种核转运蛋白分别能够识别两种类型的核定位信号(nuclear localization signal,NLS),即Kapβ1所识别的经典NLS和Kapβ2所识别的PY-NLS;然而在植物中,Kapβ2的相关研究很少。本研究在实验室已建立拟南芥cDNA文库和已有筛库结果的基础上,用酵母双杂实验进行验证,确认这些蛋白与AtTRN1(AtKapβ2)的相互作用;并进行生物信息学分析,进一步将其截短,验证截短后片段与AtTRN1的相互作用,寻找AtTRN1可能识别的区域。得到了如下结果:第一,得到了18个能够与AtTRN1相互作用的蛋白,除了2个Ran蛋白外,还有众多的酶和转录因子,同时还有一些调控蛋白、转运蛋白和1个未注释蛋白,这些蛋白均不含有PY-NLS。第二,截短实验结果及分析表明AtTRN1可能倾向于识别双组分的NLS,然而如何识别不含有双组分NLS的蛋白则依然未知。第三,AtTRN1底物的NLS没有整体碱性的特征,结构无序性较高,序列之间相似性较差。通过本论文的研究,我们得到AtTRN1与动物Kapβ2在底物类型和识别序列上诸多不同的地方。
Other AbstractResults: First we obtain 18 proteins that can interact with AtTRN1, which consist of 2 Ran proteins, many enzymes and transcription factors, some regulatory proteins, transporters and 1 protein uncharacterized. Second, the results of truncated experiment suggest AtTRN1 may be inclined to recognize bipartite NLS, however, that how AtTRN1 does recognize proteins without bipartite NLS remains unknown.
URL查看原文
Language中文
Document Type学位论文
Identifierhttps://ir.lzu.edu.cn/handle/262010/222064
Collection生命科学学院
Recommended Citation
GB/T 7714
王小宁. AtTRN1底物的NLS分析[D]. 兰州. 兰州大学,2015.
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