STRUCTURAL STUDIES OF RNASE MRP

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 核糖核酸酶MRP(RNase MRP)是一种位点特异性内切核酸酶，参与包括rRNA在内的多种RNA分子的代谢。核糖核酸酶MRP是一种核糖核蛋白复合体，它包含一个大的RNA分子和许多蛋白质组分。RNase MRP的RNA部分被认为是起催化作用的，而蛋白质组分的作用尚不清楚。阻碍对该酶进一步了解的主要问题是缺乏可用的高分辨率结构信息。目前，还没有关于RNaseMRP任何部分的结构的报道。我们的研究旨在获得关于单个组分或亚复合体的高分辨率结构信息，并最终获得RNase MRP的全酶。最近，我们已经确定RNase MRP的两个蛋白质组分Pop6和Pop7形成一个异源二聚体，与RNase MRP的RNA组分结合。我们制备了含有Pop6、Pop7及其在RNA上的结合位置的三重络合物的晶体。我们将解开这个复合体的晶体结构，以阐明这类重要的催化核糖核蛋白复合体中的RNA-蛋白质相互作用。该结构将揭示蛋白质和RNA分子在这一重要的RNA酶类中的相互作用。

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.