Gopalan Venkat, Jarrous Nayef, Krasilnikov Andrey S
Department of Chemistry and Biochemistry, Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA.
Department of Microbiology and Molecular Genetics, IMRIC, The Hebrew University-Hadassah Medical School, 91120, Jerusalem, Israel.
RNA. 2018 Jan;24(1):1-5. doi: 10.1261/rna.063107.117. Epub 2017 Sep 29.
RNase P catalyzes 5'-maturation of tRNAs in all three domains of life. This primary function is accomplished by either a ribozyme-centered ribonucleoprotein (RNP) or a protein-only variant (with one to three polypeptides). The large, multicomponent archaeal and eukaryotic RNase P RNPs appear disproportionate to the simplicity of their role in tRNA 5'-maturation, prompting the question of why the seemingly gratuitously complex RNP forms of RNase P were not replaced with simpler protein counterparts. Here, motivated by growing evidence, we consider the hypothesis that the large RNase P RNP was retained as a direct consequence of multiple roles played by its components in processes that are not related to the canonical RNase P function.
核糖核酸酶P（RNase P）催化生命三个域中转运RNA（tRNA）的5'端成熟。这一主要功能是通过以核酶为中心的核糖核蛋白（RNP）或仅含蛋白质的变体（含一至三条多肽）来完成的。大型多组分的古菌和真核生物RNase P核糖核蛋白与其在tRNA 5'端成熟中所起作用的简单性相比显得不成比例，这就引发了一个问题：为什么看似无端复杂的RNase P核糖核蛋白形式没有被更简单的蛋白质对应物所取代。在此，基于越来越多的证据，我们考虑这样一种假说，即大型RNase P核糖核蛋白得以保留，是其组分在与经典RNase P功能无关的过程中发挥多种作用的直接结果。
