Chance and necessity in the evolution of RNase P
Open Access
- 29 September 2017
- journal article
- research article
- Published by Cold Spring Harbor Laboratory in RNA
- Vol. 24 (1), 1-5
- https://doi.org/10.1261/rna.063107.117
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
Funding Information
- National Institutes of Health (GM085149, GM120582, NS096600)
- US-Israel Binational Science Foundation
- Israel Science Foundation
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