Both kinds of RNase P in all domains of life: surprises galore
- 1Department of Microbiology, The Ohio State University, Columbus, Ohio 43210, USA
- 2Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA
- 3Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA
- Corresponding author: daniels.7{at}osu.edu
Abstract
RNase P, an essential housekeeping endonuclease needed for 5′-processing of tRNAs, exists in two distinct forms: one with an RNA- and the other with a protein-based active site. The notion that the protein form of RNase P exists only in eukaryotes has been upended by the recent discovery of a protein-only variant in Bacteria and Archaea. The use of these two divergent scaffolds, shaped by convergent evolution, in all three domains of life inspires questions relating to the ancestral form of RNase P, as well as their origins and function(s) in vivo. Results from our analysis of publicly available bacterial and archaeal genomes suggest that the widespread RNA-based ribonucleoprotein variant is likely the ancient form. We also discuss the possible genetic origins and function of RNase P, including how the simultaneous presence of its variants may contribute to the fitness of their host organisms.
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Footnotes
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Article is online at http://www.rnajournal.org/cgi/doi/10.1261/rna.068379.118.
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Freely available online through the RNA Open Access option.
- Received August 9, 2018.
- Accepted December 18, 2018.
This article, published in RNA, is available undera Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/.
