Chance and necessity in the evolution of RNase P

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.

Keywords: RNase MRP; RNase P; evolution; ribonucleoprotein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Archaeal Proteins / genetics
  • Evolution, Molecular
  • Humans
  • Ribonuclease P / genetics*


  • Archaeal Proteins
  • Ribonuclease P