RNase P is an essential enzyme that catalyzes removal of the 5′ leader from precursor transfer RNAs. The ribonucleoprotein (RNP) form of RNase P is present in all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of protein cofactors. Recent cryo-electron microscopy structures of representative archaeal and eukaryotic (nuclear) RNase P holoenzymes bound to tRNA substrate/product provide high-resolution detail on subunit organization, topology, and substrate recognition in these large, multisubunit catalytic RNPs. These structures point to the challenges in understanding how proteins modulate the RNA functional repertoire and how the structure of an ancient RNA-based catalyst was reshaped during evolution by new macromolecular associations that were likely necessitated by functional/regulatory coupling.

RNase P 是一种必需的酶，可催化从前体转移 RNA 中去除 5' 前导序列。RNase P 的核糖核蛋白 (RNP) 形式存在于生命的所有领域，包含单个催化 RNA（核酶）和数量可变的蛋白质辅助因子。与 tRNA 底物/产物结合的代表性古细菌和真核生物（核）RNase P 全酶的最新冷冻电子显微镜结构提供了这些大型多亚基催化 RNP 中亚基组织、拓扑和底物识别的高分辨率细节。这些结构指出了理解蛋白质如何调节 RNA 功能库以及古老的基于 RNA 的催化剂的结构如何在进化过程中通过功能/调节耦合可能需要的新大分子关联重塑的挑战。