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Further Characterization of the Pseudo-Symmetrical Ribosomal Region

The peptidyl transferase center of the modern ribosome has been found to encompass an area of twofold pseudosymmetry (SymR). This observation strongly suggests that the very core of the ribosome arose from a dimerization event between two modest-sized RNAs. It was previously shown that at least four...

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Detalles Bibliográficos
Autores principales: Rivas, Mario, Fox, George E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555685/
https://www.ncbi.nlm.nih.gov/pubmed/32937913
http://dx.doi.org/10.3390/life10090201
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author Rivas, Mario
Fox, George E.
author_facet Rivas, Mario
Fox, George E.
author_sort Rivas, Mario
collection PubMed
description The peptidyl transferase center of the modern ribosome has been found to encompass an area of twofold pseudosymmetry (SymR). This observation strongly suggests that the very core of the ribosome arose from a dimerization event between two modest-sized RNAs. It was previously shown that at least four non-standard interactions exist between the two halves of SymR. Herein, we verify that the structure of the SymR is highly conserved with respect to both ribosome transition state and phylogenetic diversity. These comparisons also reveal two additional sites of interaction between the two halves of SymR and refine our understanding of the previously known interactions. In addition, the possible role that magnesium may have in the coordination, stabilization, association, and evolutionary history of the two halves (A-region and P-region) was examined. Together, the results identify a likely site where structural elements and Mg(2+) ions may have facilitated the ligation of two aboriginal RNAs into a single unit.
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spelling pubmed-75556852020-10-19 Further Characterization of the Pseudo-Symmetrical Ribosomal Region Rivas, Mario Fox, George E. Life (Basel) Article The peptidyl transferase center of the modern ribosome has been found to encompass an area of twofold pseudosymmetry (SymR). This observation strongly suggests that the very core of the ribosome arose from a dimerization event between two modest-sized RNAs. It was previously shown that at least four non-standard interactions exist between the two halves of SymR. Herein, we verify that the structure of the SymR is highly conserved with respect to both ribosome transition state and phylogenetic diversity. These comparisons also reveal two additional sites of interaction between the two halves of SymR and refine our understanding of the previously known interactions. In addition, the possible role that magnesium may have in the coordination, stabilization, association, and evolutionary history of the two halves (A-region and P-region) was examined. Together, the results identify a likely site where structural elements and Mg(2+) ions may have facilitated the ligation of two aboriginal RNAs into a single unit. MDPI 2020-09-14 /pmc/articles/PMC7555685/ /pubmed/32937913 http://dx.doi.org/10.3390/life10090201 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Rivas, Mario
Fox, George E.
Further Characterization of the Pseudo-Symmetrical Ribosomal Region
title Further Characterization of the Pseudo-Symmetrical Ribosomal Region
title_full Further Characterization of the Pseudo-Symmetrical Ribosomal Region
title_fullStr Further Characterization of the Pseudo-Symmetrical Ribosomal Region
title_full_unstemmed Further Characterization of the Pseudo-Symmetrical Ribosomal Region
title_short Further Characterization of the Pseudo-Symmetrical Ribosomal Region
title_sort further characterization of the pseudo-symmetrical ribosomal region
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555685/
https://www.ncbi.nlm.nih.gov/pubmed/32937913
http://dx.doi.org/10.3390/life10090201
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