RNase MRP是广泛存在于真核生物中，为生命活动所必需的一类核酸内切酶，其参与了体内大量RNA分子的加工代谢活动。它是由近十个蛋白质亚基和一个具有催化活性的RNA亚基组成的极其复杂的核糖核酸蛋白质复合物。在进化上，RNase MRP是由RNase P 衍生而来，与RNase P在组成上也高度相关，除了RNA亚基保留了核心的催化结构域外，两者在蛋白质构成上也共享了很多蛋白质亚基。但是，RNase MRP却具有完全不同于RNase P的生物学功能。其主要负责切割核糖体成熟过程中的rRNA前体。目前我们对于真核生物的RNase MRP的全酶结构，底物识别乃至底物催化的切割机制都还所知甚少。本项目聚焦酵母RNase MRP全酶及底物结合状态的结构，期望在原子尺度阐释RNase MRP各亚基的空间关系及其发挥催化活性的分子机理。

Ribonuclease (RNase) MRP is a ubiquitous and essential site-specific eukaryotic endoribonuclease involved in the metabolism of a wide range of RNA molecules. RNase MRP is a ribonucleoprotein complex containing about ten protein subunits and one catalytic RNA subunit. RNase MRP is evolved from RNase P and closely related to the RNA component of RNase P, and multiple proteins, most of which are shared with RNase P. RNase MRP possesses a distinct function that different from RNase P, and mainly involved in the processing of the pre-rRNA in the ribosome assembly pathway. Currently, structures of the RNase MRP holoenzyme, and substrate recognition and processing mechanism are still poorly understood. This project will focus on the understanding of the holoenzyme and substrate-bound structures，the spacial organization, the catalytic mechanism of RNase MRP at an atomic level.