STRUCTURAL STUDIES OF RNASE MRP

RNA酶 MRP 的结构研究

• 批准号: 7957302
• 负责人: ANDREY S. KRASILNIKOV
• 金额: $ 0.48万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-07-01 至 2010-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7957302
• 关键词: Binding Sites; Catalysis; Complex; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Endoribonucleases; Enzymes; Funding; Grant; Holoenzymes; Individual; Institution; Light; Metabolism; Proteins; RNA; RNA Binding; RNA-Protein Interaction; RNAse MRP; Reporting; Research; Research Personnel; Resolution; Resources; Ribonucleases; Ribonucleoproteins; Ribosomal RNA; Role; Site; Source; Structure; Synchrotrons; United States National Institutes of Health; base; endoribonuclease; numb protein

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Ribonuclease MRP (RNase MRP) is a site-specific endoribonuclease involved in metabolism of various RNA molecules including rRNA. RNase MRP is a ribonucleoprotein complex which contains a large RNA molecule and a number of protein components. The RNA moiety of RNase MRP is presumed be responsible for catalysis, while the role of the protein components is not clear. The major problem that hinders further understanding of this enzyme is the absence of available high-resolution structural information. At this moment, there are no reported structures of any part of RNase MRP. Our research is aimed at obtaining high-resolution structural information on the individual components or subcomplexes and, eventually, the holoenzyme of RNase MRP. Recently, we have established that two of the protein components of RNase MRP, Pop6 and Pop7, form a heterodimer which binds the RNA component of RNase MRP. We produced crystals of this triple complex containing Pop6, Pop7 and their binding site on RNA. We will solve the crystal structure of this complex to shed light on the RNA-protein interactions in this important class of catalytic ribonucleoprotein complexes. The structure will reveal the interplay between protein and RNA molecules in this important class of RNA-based enzymes.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 核糖核酸酶MRP（RNase MRP）是一种参与包括rRNA在内的各种RNA分子代谢的位点特异性核糖核酸内切酶。RNase MRP是一种核糖核蛋白复合物，它含有一个大的RNA分子和许多蛋白质组分。推测RNase MRP的RNA部分负责催化，而蛋白质组分的作用尚不清楚。阻碍进一步了解这种酶的主要问题是缺乏可用的高分辨率结构信息。目前，还没有报道RNase MRP任何部分的结构。我们的研究旨在获得高分辨率的结构信息的各个组成部分或亚复合物，并最终RNase MRP的全酶。最近，我们已经确定了RNase MRP的两种蛋白质组分Pop 6和Pop 7形成异二聚体，其结合RNase MRP的RNA组分。我们生产了这种含有Pop 6、Pop 7及其在RNA上结合位点的三重复合物的晶体。我们将解决这个复杂的晶体结构，揭示在这类重要的催化核糖核蛋白复合物的RNA-蛋白质相互作用。该结构将揭示蛋白质和RNA分子之间的相互作用，在这类重要的基于RNA的酶。