ArticlePLoS genetics2014
Playing RNase P evolution: swapping the RNA catalyst for a protein reveals functional uniformity of highly divergent enzyme forms.
Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- Bacterial/archaeal protein-only RNase P: complementation inRNA (New York, N.Y.) · 2025Article
- Composition and RNA binding specificity of metazoan RNase MRP.Nucleic acids research · 2025Article
- The Constructive Neutral Evolution of Behaviour.Ecology and evolution · 2025Article
- Suppression of theRNA (New York, N.Y.) · 2024Article
- Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes.The Journal of biological chemistry · 2024Review
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
- Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA.Nucleic acids research · 2020Article
- Both kinds of RNase P in all domains of life: surprises galore.RNA (New York, N.Y.) · 2019Article
- Distributive enzyme binding controlled by local RNA context results in 3' to 5' directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P.Nucleic acids research · 2019Article
- Biochemical Studies Provide Insights into the Necessity for Multiple Arabidopsis thaliana Protein-Only RNase P Isoenzymes.Journal of molecular biology · 2019Article
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
- Minimal and RNA-free RNase P inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Protein-only RNase P function in Escherichia coli: viability, processing defects and differences between PRORP isoenzymes.Nucleic acids research · 2017Article
- Repairing tRNA termini: News from the 3' end.RNA biology · 2016Article
- Mechanistic and Structural Studies of Protein-Only RNase P Compared to Ribonucleoproteins Reveal the Two Faces of the Same Enzymatic Activity.Biomolecules · 2016Review
- Use of chemical modification and mass spectrometry to identify substrate-contacting sites in proteinaceous RNase P, a tRNA processing enzyme.Nucleic acids research · 2016Article
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P.Nucleic acids research · 2016Article
- RNase P-Mediated Sequence-Specific Cleavage of RNA by Engineered External Guide Sequences.Biomolecules · 2015Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The RNase P family is a diverse group of endonucleases responsible for the removal of 5' extensions from tRNA precursors. The diversity of enzyme forms finds its extremes in the eukaryal nucleus where RNA-based catalysis by complex ribonucleoproteins in some organisms contrasts with single-polypeptide enzymes in others. Such structural contrast suggests associated functional differences, and the complexity of the ribonucleoprotein was indeed proposed to broaden the enzyme's functionality beyond tRNA processing. To explore functional overlap and differences between most divergent forms of RNase P, we replaced the nuclear RNase P of Saccharomyces cerevisiae, a 10-subunit ribonucleoprotein, with Arabidopsis thaliana PRORP3, a single monomeric protein. Surprisingly, the RNase P-swapped yeast strains were viable, displayed essentially unimpaired growth under a wide variety of conditions, and, in a certain genetic background, their fitness even slightly exceeded that of the wild type. The molecular analysis of the RNase P-swapped strains showed a minor disturbance in tRNA metabolism, but did not point to any RNase P substrates or functions beyond that. Altogether, these results indicate the full functional exchangeability of the highly dissimilar enzymes. Our study thereby establishes the RNase P family, with its combination of structural diversity and functional uniformity, as an extreme case of convergent evolution. It moreover suggests that the apparently gratuitous complexity of some RNase P forms is the result of constructive neutral evolution rather than reflecting increased functional versatility.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.