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The multistructural forms of box C/D ribonucleoprotein particles

Structural biology studies of archaeal and yeast box C/D ribonucleoprotein particles (RNPs) reveal a surprisingly wide range of forms. If form ever follows function, the different structures of box C/D small ribonucleoprotein particles (snoRNPs) may reflect their versatile functional roles beyond wh...

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Detalles Bibliográficos
Autores principales: Yu, Ge, Zhao, Yu, Li, Hong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6239191/
https://www.ncbi.nlm.nih.gov/pubmed/30254138
http://dx.doi.org/10.1261/rna.068312.118
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author Yu, Ge
Zhao, Yu
Li, Hong
author_facet Yu, Ge
Zhao, Yu
Li, Hong
author_sort Yu, Ge
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description Structural biology studies of archaeal and yeast box C/D ribonucleoprotein particles (RNPs) reveal a surprisingly wide range of forms. If form ever follows function, the different structures of box C/D small ribonucleoprotein particles (snoRNPs) may reflect their versatile functional roles beyond what has been recognized. A large majority of box C/D RNPs serve to site-specifically methylate the ribosomal RNA, typically as independent complexes. Select members of the box C/D snoRNPs also are essential components of the megadalton RNP enzyme, the small subunit processome that is responsible for processing ribosomal RNA. Other box C/D RNPs continue to be uncovered with either unexpected or unknown functions. We summarize currently known box C/D RNP structures in this review and identify the Nop56/58 and box C/D RNA subunits as the key elements underlying the observed structural diversity, and likely, the diverse functional roles of box C/D RNPs.
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spelling pubmed-62391912019-12-01 The multistructural forms of box C/D ribonucleoprotein particles Yu, Ge Zhao, Yu Li, Hong RNA Review Structural biology studies of archaeal and yeast box C/D ribonucleoprotein particles (RNPs) reveal a surprisingly wide range of forms. If form ever follows function, the different structures of box C/D small ribonucleoprotein particles (snoRNPs) may reflect their versatile functional roles beyond what has been recognized. A large majority of box C/D RNPs serve to site-specifically methylate the ribosomal RNA, typically as independent complexes. Select members of the box C/D snoRNPs also are essential components of the megadalton RNP enzyme, the small subunit processome that is responsible for processing ribosomal RNA. Other box C/D RNPs continue to be uncovered with either unexpected or unknown functions. We summarize currently known box C/D RNP structures in this review and identify the Nop56/58 and box C/D RNA subunits as the key elements underlying the observed structural diversity, and likely, the diverse functional roles of box C/D RNPs. Cold Spring Harbor Laboratory Press 2018-12 /pmc/articles/PMC6239191/ /pubmed/30254138 http://dx.doi.org/10.1261/rna.068312.118 Text en © 2018 Yu 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 Review
Yu, Ge
Zhao, Yu
Li, Hong
The multistructural forms of box C/D ribonucleoprotein particles
title The multistructural forms of box C/D ribonucleoprotein particles
title_full The multistructural forms of box C/D ribonucleoprotein particles
title_fullStr The multistructural forms of box C/D ribonucleoprotein particles
title_full_unstemmed The multistructural forms of box C/D ribonucleoprotein particles
title_short The multistructural forms of box C/D ribonucleoprotein particles
title_sort multistructural forms of box c/d ribonucleoprotein particles
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6239191/
https://www.ncbi.nlm.nih.gov/pubmed/30254138
http://dx.doi.org/10.1261/rna.068312.118
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