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.
Bibliographical noteFunding Information:
We thank Phil Bevilacqua (Penn State) for valuable comments and suggestions. We are grateful to Sara Lung (OSU) for assistance with preparation of the figure, and Lien Lai (OSU) for help and input with this illustration. A.K., N.J., and V.G. gratefully acknowledge funding for their research from the National Institutes of Health (GM085149 [A.K.], GM120582 [V.G.], and NS096600 [V.G.]), the US-Israel Binational Science Foundation (#2015/157 [N.J., V.G.]), and the Israel Science Foundation (#1205/2017 [N.J.]).
© 2018 Gopalan et al.
- RNase MRP
- RNase P