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Both kinds of RNase P in all domains of life: surprises galore
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 protei...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6380272/ https://www.ncbi.nlm.nih.gov/pubmed/30578286 http://dx.doi.org/10.1261/rna.068379.118 |
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author | Daniels, Charles J. Lai, Lien B. Chen, Tien-Hao Gopalan, Venkat |
author_facet | Daniels, Charles J. Lai, Lien B. Chen, Tien-Hao Gopalan, Venkat |
author_sort | Daniels, Charles J. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6380272 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-63802722019-03-09 Both kinds of RNase P in all domains of life: surprises galore Daniels, Charles J. Lai, Lien B. Chen, Tien-Hao Gopalan, Venkat RNA Letter to the Editor 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. Cold Spring Harbor Laboratory Press 2019-03 /pmc/articles/PMC6380272/ /pubmed/30578286 http://dx.doi.org/10.1261/rna.068379.118 Text en © 2019 Daniels et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by/4.0/ 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/. |
spellingShingle | Letter to the Editor Daniels, Charles J. Lai, Lien B. Chen, Tien-Hao Gopalan, Venkat Both kinds of RNase P in all domains of life: surprises galore |
title | Both kinds of RNase P in all domains of life: surprises galore |
title_full | Both kinds of RNase P in all domains of life: surprises galore |
title_fullStr | Both kinds of RNase P in all domains of life: surprises galore |
title_full_unstemmed | Both kinds of RNase P in all domains of life: surprises galore |
title_short | Both kinds of RNase P in all domains of life: surprises galore |
title_sort | both kinds of rnase p in all domains of life: surprises galore |
topic | Letter to the Editor |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6380272/ https://www.ncbi.nlm.nih.gov/pubmed/30578286 http://dx.doi.org/10.1261/rna.068379.118 |
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