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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 核糖核酸酶MRP（RNase MRP）是一种特定于位点的内核酸酶，参与包括RRNA在内的各种RNA分子的代谢。 RNase MRP是一种核糖核蛋白复合物，其中包含大的RNA分子和许多蛋白质成分。假定RNase MRP的RNA部分是负责催化的，而蛋白质成分的作用尚不清楚。阻碍对该酶的进一步理解的主要问题是没有可用的高分辨率结构信息。目前，尚无RNase MRP任何部分的报告结构。我们的研究旨在获得有关单个组件或子复合物的高分辨率结构信息，并最终获得RNase MRP的全酶。最近，我们确定RNase MRP，POP6和POP7的两个蛋白质成分形成了一种结合RNase MRP的RNA成分的异二聚体。我们在RNA上产生了包含POP6，POP7及其结合位点的三重复合物的晶体。我们将在这一重要类型的催化核糖核蛋白复合物中解决该复合物的晶体结构，从而阐明RNA-蛋白质相互作用。该结构将在这类基于RNA的酶中揭示蛋白质和RNA分子之间的相互作用。