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The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold
Exoribonuclease-resistant RNAs (xrRNAs) are discrete elements that block the progression of 5′ to 3′ exoribonucleases using specifically folded RNA structures. A recently discovered class of xrRNA is widespread in several genera of plant-infecting viruses, within both noncoding and protein-coding su...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7668246/ https://www.ncbi.nlm.nih.gov/pubmed/32848042 http://dx.doi.org/10.1261/rna.076224.120 |
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author | Steckelberg, Anna-Lena Vicens, Quentin Costantino, David A. Nix, Jay C. Kieft, Jeffrey S. |
author_facet | Steckelberg, Anna-Lena Vicens, Quentin Costantino, David A. Nix, Jay C. Kieft, Jeffrey S. |
author_sort | Steckelberg, Anna-Lena |
collection | PubMed |
description | Exoribonuclease-resistant RNAs (xrRNAs) are discrete elements that block the progression of 5′ to 3′ exoribonucleases using specifically folded RNA structures. A recently discovered class of xrRNA is widespread in several genera of plant-infecting viruses, within both noncoding and protein-coding subgenomic RNAs. The structure of one such xrRNA from a dianthovirus revealed three-dimensional details of the resistant fold but did not answer all questions regarding the conservation and diversity of this xrRNA class. Here, we present the crystal structure of a representative polerovirus xrRNA that contains sequence elements that diverge from the previously solved structure. This new structure rationalizes previously unexplained sequence conservation patterns and shows interactions not present in the first structure. Together, the structures of these xrRNAs from dianthovirus and polerovirus genera support the idea that these plant virus xrRNAs fold through a defined pathway that includes a programmed intermediate conformation. This work deepens our knowledge of the structure–function relationship of xrRNAs and shows how evolution can craft similar RNA folds from divergent sequences. |
format | Online Article Text |
id | pubmed-7668246 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-76682462021-12-01 The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold Steckelberg, Anna-Lena Vicens, Quentin Costantino, David A. Nix, Jay C. Kieft, Jeffrey S. RNA Report Exoribonuclease-resistant RNAs (xrRNAs) are discrete elements that block the progression of 5′ to 3′ exoribonucleases using specifically folded RNA structures. A recently discovered class of xrRNA is widespread in several genera of plant-infecting viruses, within both noncoding and protein-coding subgenomic RNAs. The structure of one such xrRNA from a dianthovirus revealed three-dimensional details of the resistant fold but did not answer all questions regarding the conservation and diversity of this xrRNA class. Here, we present the crystal structure of a representative polerovirus xrRNA that contains sequence elements that diverge from the previously solved structure. This new structure rationalizes previously unexplained sequence conservation patterns and shows interactions not present in the first structure. Together, the structures of these xrRNAs from dianthovirus and polerovirus genera support the idea that these plant virus xrRNAs fold through a defined pathway that includes a programmed intermediate conformation. This work deepens our knowledge of the structure–function relationship of xrRNAs and shows how evolution can craft similar RNA folds from divergent sequences. Cold Spring Harbor Laboratory Press 2020-12 /pmc/articles/PMC7668246/ /pubmed/32848042 http://dx.doi.org/10.1261/rna.076224.120 Text en © 2020 Steckelberg et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Report Steckelberg, Anna-Lena Vicens, Quentin Costantino, David A. Nix, Jay C. Kieft, Jeffrey S. The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold |
title | The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold |
title_full | The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold |
title_fullStr | The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold |
title_full_unstemmed | The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold |
title_short | The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold |
title_sort | crystal structure of a polerovirus exoribonuclease-resistant rna shows how diverse sequences are integrated into a conserved fold |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7668246/ https://www.ncbi.nlm.nih.gov/pubmed/32848042 http://dx.doi.org/10.1261/rna.076224.120 |
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