Chance and necessity in the evolution of RNase P
- ↵* Corresponding author; email: ask11{at}psu.edu
Abstract
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
- Received July 23, 2017.
- Accepted September 22, 2017.
- Published by Cold Spring Harbor Laboratory Press for the RNA Society
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