兰州大学机构库 >生命科学学院
核糖体蛋白S10的甲基化对其与B23相互作用的影响
Alternative TitleMethylation of Ribosomal Protein S10 Affects its Interaction with B23
梁雨横
Thesis Advisor刘恒
2009-05-25
Degree Grantor兰州大学
Place of Conferral兰州
Degree Name硕士
Keyword核糖体 精氨酸甲基化转移酶5 蛋白质甲基化 核糖体蛋白S10
Abstract核糖体负责细胞内蛋白质的合成,其数量和状态跟细胞的生长密切相关。研究表明,核糖体复合体亚基的蛋白很多是被翻译后修饰的,包括磷酸化,甲基化和乙酰化等,这些修饰会影响核糖体的发生或功能,从而调控细胞的生长增殖。核糖体蛋白的甲基化修饰,包括精氨酸残基和赖氨酸残基的甲基化修饰,而精氨酸的ω-NG的甲基化是由蛋白质精氨酸甲基化转移酶 (Protein arginine methyltransferase, PRMTs)催化形成的。蛋白质精氨酸甲基化转移酶5 (Protein arginine methyltransferase 5, PRMT5)是甲基化转移酶家族成员之一,可以通过对底物蛋白质的精氨酸甲基化修饰来调节其功能。 我们先前的研究已证明,核糖体蛋白S10(Ribosomal Protein S10,RPS10)在核内定位于核仁区域,57%集中在核仁颗粒组分区,其余的43%定位于核仁致密纤维组分区;而R158/160K突变体则全部集中于核仁致密纤维组分区。本研究的结论:I. 通过甲基化实验,发现PRMT5能甲基化RPS10的158和160位精氨酸。II. 应用免疫共沉淀实验证明,RPS10是一个新的B23结合蛋白,GST pull-down实验表明这种结合是直接的;而R158/160K甲基化突变体与B23的结合能力减弱。而B23是核仁颗粒组分区的标志蛋白,跟更重要的是,它是一个在核糖体发生中具有重要作用的蛋白。这项研究说明,B23能够选择性的结合甲基化的RPS10,并将其存储在核仁颗粒区。 综上所述,PRMT5可能通过甲基化修饰核糖体蛋白S10,从而影响其与B23蛋白的相互作用,以实现该甲基化酶的下游功能的调节。
Other AbstractRibosomes are responsible for the synthesis of polypeptide chains and its biogenesis is thus a critical process inextricably linked to cell growth and proliferation. Post-translational modifications of ribosomal proteins, including phosphorylation, methylation and acetylation, affect the ribosome biogenesis or activity. Protein arginine methyltransferases (PRMTs) are enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (SAM) to arginine. Protein Arginine Methyltransferase 5 (PRMT5) is a member of PRMTs family. PRMT5 regulates other proteins’ function through methylation a subset of substrates. In our previous experiments, 57% Ribosomal Protein S10 (RPS10) localizes in the granular component region (GC) in nucleus and the rest concentrates in dense fibrillar component region (DFC). However, RPS10 methylation mutant R158/160K solely concentrates in DFC region. The major results were as follows: I. We found PRMT5 catalyzes RPS10 methylation at Arg158 and Arg160 residues. II. Using co-immunoprecipitation we found RPS10 is a novel B23 binding protein, and this binding is proved to be direct through GST-pull down. Moreover, RPS10 methylation mutant interacts weakly with B23. And B23 is the mark protein of Granular component region in nucleus, and plays a vital role in ribosome biogenesis. So, we can say that B23 may bind to RPS10 methylated and store it in the GC region in nucleus. Together, we deduce that PRMT5 may play the multiple functions through methylating RPS10 and affect its interaction with B23.
URL查看原文
Language中文
Document Type学位论文
Identifierhttps://ir.lzu.edu.cn/handle/262010/221249
Collection生命科学学院
Recommended Citation
GB/T 7714
梁雨横. 核糖体蛋白S10的甲基化对其与B23相互作用的影响[D]. 兰州. 兰州大学,2009.
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