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Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly
Here we report the crystal structures of the Thermus thermophilus ribosome at 2.3-2.5Å-resolution, which have enabled a comprehensive modeling of rRNA modifications. The structures reveal contacts of modified nucleotides with mRNA and tRNAs or protein pY, and contacts within the ribosome interior st...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401423/ https://www.ncbi.nlm.nih.gov/pubmed/25775268 http://dx.doi.org/10.1038/nsmb.2992 |
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author | Polikanov, Yury S. Melnikov, Sergey V. Söll, Dieter Steitz, Thomas A. |
author_facet | Polikanov, Yury S. Melnikov, Sergey V. Söll, Dieter Steitz, Thomas A. |
author_sort | Polikanov, Yury S. |
collection | PubMed |
description | Here we report the crystal structures of the Thermus thermophilus ribosome at 2.3-2.5Å-resolution, which have enabled a comprehensive modeling of rRNA modifications. The structures reveal contacts of modified nucleotides with mRNA and tRNAs or protein pY, and contacts within the ribosome interior stabilizing the functional fold of rRNA. Our work provides a resource to explore the roles of rRNA modifications and yields the most complete atomic model of bacterial ribosome. |
format | Online Article Text |
id | pubmed-4401423 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
record_format | MEDLINE/PubMed |
spelling | pubmed-44014232015-10-01 Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly Polikanov, Yury S. Melnikov, Sergey V. Söll, Dieter Steitz, Thomas A. Nat Struct Mol Biol Article Here we report the crystal structures of the Thermus thermophilus ribosome at 2.3-2.5Å-resolution, which have enabled a comprehensive modeling of rRNA modifications. The structures reveal contacts of modified nucleotides with mRNA and tRNAs or protein pY, and contacts within the ribosome interior stabilizing the functional fold of rRNA. Our work provides a resource to explore the roles of rRNA modifications and yields the most complete atomic model of bacterial ribosome. 2015-03-16 2015-04 /pmc/articles/PMC4401423/ /pubmed/25775268 http://dx.doi.org/10.1038/nsmb.2992 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Polikanov, Yury S. Melnikov, Sergey V. Söll, Dieter Steitz, Thomas A. Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly |
title | Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly |
title_full | Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly |
title_fullStr | Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly |
title_full_unstemmed | Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly |
title_short | Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly |
title_sort | structural insights into the role of rrna modifications in protein synthesis and ribosome assembly |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401423/ https://www.ncbi.nlm.nih.gov/pubmed/25775268 http://dx.doi.org/10.1038/nsmb.2992 |
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