Smith J Kristin, Hsieh John, Fierke Carol A
Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109, USA.
Biopolymers. 2007;87(5-6):329-38. doi: 10.1002/bip.20846.
Ribonuclease P (RNase P) is a ribonucleoprotein (RNP) complex that catalyzes the metal-dependent maturation of the 5' end of precursor tRNAs (pre-tRNAs) in all organisms. RNase P is comprised of a catalytic RNA (P RNA), and at least one essential protein (P protein). Although P RNA is the catalytic subunit of the enzyme and is active in the absence of P protein under high salt concentrations in vitro, the protein is still required for enzyme activity in vivo. Therefore, the function of the P protein and how it interacts with both P RNA and pre-tRNA have been the focus of much ongoing research. RNA-protein interactions in RNase P serve a number of critical roles in the RNP including stabilizing the structure, and enhancing the affinity for substrates and metal ions. This review examines the role of RNA-protein interactions in bacterial RNase P from both structural and mechanistic perspectives.
核糖核酸酶P（RNase P）是一种核糖核蛋白（RNP）复合物，可催化所有生物体中前体tRNA（pre-tRNA）5'端的金属依赖性成熟。RNase P由催化性RNA（P RNA）和至少一种必需蛋白（P蛋白）组成。尽管P RNA是该酶的催化亚基，并且在体外高盐浓度下无P蛋白时具有活性，但体内酶活性仍需要该蛋白。因此，P蛋白的功能及其与P RNA和pre-tRNA的相互作用方式一直是许多正在进行的研究的重点。RNase P中的RNA-蛋白质相互作用在RNP中发挥着许多关键作用，包括稳定结构、增强对底物和金属离子的亲和力。本综述从结构和机制角度探讨了RNA-蛋白质相互作用在细菌RNase P中的作用。
