Chance and necessity in the evolution of RNase P

Venkat Gopalan*, Nayef Jarrous, Andrey S. Krasilnikov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


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.

Original languageAmerican English
Pages (from-to)1-5
Number of pages5
Issue number1
StatePublished - Jan 2018

Bibliographical note

Publisher Copyright:
© 2018 Gopalan et al.


  • Evolution
  • RNase MRP
  • RNase P
  • Ribonucleoprotein


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