Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Polikanov, Yury S., Melnikov, Sergey V., Söll, Dieter, Steitz, Thomas A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
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
_version_ 1782367142652411904
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
work_keys_str_mv AT polikanovyurys structuralinsightsintotheroleofrrnamodificationsinproteinsynthesisandribosomeassembly
AT melnikovsergeyv structuralinsightsintotheroleofrrnamodificationsinproteinsynthesisandribosomeassembly
AT solldieter structuralinsightsintotheroleofrrnamodificationsinproteinsynthesisandribosomeassembly
AT steitzthomasa structuralinsightsintotheroleofrrnamodificationsinproteinsynthesisandribosomeassembly