Crystallographic studies on UNR, a protein important for translation and decay of mRNA, and on the RNA-induced silencing complex RISC
UNR(一种对 mRNA 翻译和衰变很重要的蛋白质)以及 RNA 诱导的沉默复合物 RISC 的晶体学研究
基本信息
- 批准号:47407147
- 负责人:
- 金额:--
- 依托单位:
- 依托单位国家:德国
- 项目类别:Research Units
- 财政年份:2007
- 资助国家:德国
- 起止时间:2006-12-31 至 2010-12-31
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
The RNA-binding protein UNR is involved in the IRES-mediated initiation of mRNA translation, the mCRD-dependent decay of mRNA, and in the inhibition of msl2-mRNA translation as co-repressor of the sex-lethal protein. UNR binds directly to the IRES- or the mCRD-element of mRNAs, and UNR is also capable to form RNA-free complexes with other proteins like the Poly(A)-binding protein, the UNR-interacting protein (UNRIP), and the sex-lethal protein. UNR consists of five cold shock domains, but their role with respect to the different functional complexes has to be elucidated. In order to understand the structural basis for the versatile functions of UNR we want to determine the three-dimensional structure of UNR and of functional UNR-containing proteinprotein or protein-RNA complexes by means of X-ray crystallography. A second project concerns the preparation, crystallization and crystal structure determination of an RNA-induced silencing complex (RISC), which plays a central role in the control of gene expression by RNA interference. A minimal human RISC, formed by the proteins Dicer, Argonaute2 and TRBP, was shown to exhibit dsRNA loading, strand selection, and target mRNA cleavage activities. We will establish a eukaryotic co-expression system in order to obtain reasonable amounts of the heterotrimeric protein complex for crystallization experiments. Major aim is the crystal structure analysis of the minimal RISC in different functional states. Additionally, this recombinant minimal RISC will be used for single particle cryo-electron microscopy studies.
rna结合蛋白UNR参与ires介导的mRNA翻译起始,mcrd依赖性mRNA衰变,以及作为性致死蛋白的共同抑制因子抑制msl2-mRNA翻译。UNR直接与mrna的IRES-或mcrd -元件结合,并且UNR还能够与其他蛋白质如Poly(A)结合蛋白、UNR相互作用蛋白(UNRIP)和性致死蛋白形成无rna复合物。UNR由五个冷冲击域组成,但它们对不同功能复合物的作用必须加以阐明。为了了解UNR多功能的结构基础,我们想用x射线晶体学的方法确定UNR的三维结构以及含有UNR的功能性蛋白质或蛋白质- rna复合物的三维结构。第二个项目涉及RNA诱导沉默复合体(RISC)的制备、结晶和晶体结构确定,该复合体在通过RNA干扰控制基因表达中起核心作用。由Dicer、Argonaute2和TRBP蛋白组成的最小人类RISC被证明具有dsRNA装载、链选择和靶mRNA切割活性。为了获得合理数量的异三聚体蛋白复合体用于结晶实验,我们将建立真核共表达系统。主要目的是分析最小RISC在不同功能状态下的晶体结构。此外,该重组最小RISC将用于单粒子低温电子显微镜研究。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Professor Dr. Ralf Ficner其他文献
Professor Dr. Ralf Ficner的其他文献
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{{ truncateString('Professor Dr. Ralf Ficner', 18)}}的其他基金
Structural and functional analysis of the tRNA-modifying enzymes DNMT2 and tRNA-guanine-transglycosylase
tRNA 修饰酶 DNMT2 和 tRNA-鸟嘌呤转糖基酶的结构和功能分析
- 批准号:
277404908 - 财政年份:2015
- 资助金额:
-- - 项目类别:
Priority Programmes
X-ray crystallographic structure analysis of the RNA thermometer ROSE and the preQ1-specific riboswitch
RNA温度计ROSE和preQ1特异性核糖开关的X射线晶体结构分析
- 批准号:
39952435 - 财政年份:2007
- 资助金额:
-- - 项目类别:
Priority Programmes
Crystallographic studies on snRNP-and SMN-Associated DExD/H-box proteins and on the editosome-specific nuclease TbMP42
snRNP 和 SMN 相关 DExD/H-box 蛋白以及编辑体特异性核酸酶 TbMP42 的晶体学研究
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5423728 - 财政年份:2004
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-- - 项目类别:
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