Cargando…
Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM
The extent of ribosomal heterogeneity has caught increasing interest over the past few years, as recent studies have highlighted the presence of structural variations of the ribosome. More precisely, the heterogeneity of the ribosome covers multiple scales, including the dynamical aspects of ribosom...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7570653/ https://www.ncbi.nlm.nih.gov/pubmed/32957592 http://dx.doi.org/10.3390/molecules25184262 |
_version_ | 1783596996673667072 |
---|---|
author | Poitevin, Frédéric Kushner, Artem Li, Xinpei Dao Duc, Khanh |
author_facet | Poitevin, Frédéric Kushner, Artem Li, Xinpei Dao Duc, Khanh |
author_sort | Poitevin, Frédéric |
collection | PubMed |
description | The extent of ribosomal heterogeneity has caught increasing interest over the past few years, as recent studies have highlighted the presence of structural variations of the ribosome. More precisely, the heterogeneity of the ribosome covers multiple scales, including the dynamical aspects of ribosomal motion at the single particle level, specialization at the cellular and subcellular scale, or evolutionary differences across species. Upon solving the ribosome atomic structure at medium to high resolution, cryogenic electron microscopy (cryo-EM) has enabled investigating all these forms of heterogeneity. In this review, we present some recent advances in quantifying ribosome heterogeneity, with a focus on the conformational and evolutionary variations of the ribosome and their functional implications. These efforts highlight the need for new computational methods and comparative tools, to comprehensively model the continuous conformational transition pathways of the ribosome, as well as its evolution. While developing these methods presents some important challenges, it also provides an opportunity to extend our interpretation and usage of cryo-EM data, which would more generally benefit the study of molecular dynamics and evolution of proteins and other complexes. |
format | Online Article Text |
id | pubmed-7570653 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-75706532020-10-28 Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM Poitevin, Frédéric Kushner, Artem Li, Xinpei Dao Duc, Khanh Molecules Review The extent of ribosomal heterogeneity has caught increasing interest over the past few years, as recent studies have highlighted the presence of structural variations of the ribosome. More precisely, the heterogeneity of the ribosome covers multiple scales, including the dynamical aspects of ribosomal motion at the single particle level, specialization at the cellular and subcellular scale, or evolutionary differences across species. Upon solving the ribosome atomic structure at medium to high resolution, cryogenic electron microscopy (cryo-EM) has enabled investigating all these forms of heterogeneity. In this review, we present some recent advances in quantifying ribosome heterogeneity, with a focus on the conformational and evolutionary variations of the ribosome and their functional implications. These efforts highlight the need for new computational methods and comparative tools, to comprehensively model the continuous conformational transition pathways of the ribosome, as well as its evolution. While developing these methods presents some important challenges, it also provides an opportunity to extend our interpretation and usage of cryo-EM data, which would more generally benefit the study of molecular dynamics and evolution of proteins and other complexes. MDPI 2020-09-17 /pmc/articles/PMC7570653/ /pubmed/32957592 http://dx.doi.org/10.3390/molecules25184262 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 | Review Poitevin, Frédéric Kushner, Artem Li, Xinpei Dao Duc, Khanh Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM |
title | Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM |
title_full | Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM |
title_fullStr | Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM |
title_full_unstemmed | Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM |
title_short | Structural Heterogeneities of the Ribosome: New Frontiers and Opportunities for Cryo-EM |
title_sort | structural heterogeneities of the ribosome: new frontiers and opportunities for cryo-em |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7570653/ https://www.ncbi.nlm.nih.gov/pubmed/32957592 http://dx.doi.org/10.3390/molecules25184262 |
work_keys_str_mv | AT poitevinfrederic structuralheterogeneitiesoftheribosomenewfrontiersandopportunitiesforcryoem AT kushnerartem structuralheterogeneitiesoftheribosomenewfrontiersandopportunitiesforcryoem AT lixinpei structuralheterogeneitiesoftheribosomenewfrontiersandopportunitiesforcryoem AT daoduckhanh structuralheterogeneitiesoftheribosomenewfrontiersandopportunitiesforcryoem |