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The central role of protein S12 in organizing the structure of the decoding site of the ribosome
The ribosome decodes mRNA by monitoring the geometry of codon–anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallography, we have determined that conditional-lethal, st...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3884664/ https://www.ncbi.nlm.nih.gov/pubmed/24152548 http://dx.doi.org/10.1261/rna.040030.113 |
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author | Demirci, Hasan Wang, Leyi Murphy, Frank V. Murphy, Eileen L. Carr, Jennifer F. Blanchard, Scott C. Jogl, Gerwald Dahlberg, Albert E. Gregory, Steven T. |
author_facet | Demirci, Hasan Wang, Leyi Murphy, Frank V. Murphy, Eileen L. Carr, Jennifer F. Blanchard, Scott C. Jogl, Gerwald Dahlberg, Albert E. Gregory, Steven T. |
author_sort | Demirci, Hasan |
collection | PubMed |
description | The ribosome decodes mRNA by monitoring the geometry of codon–anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallography, we have determined that conditional-lethal, streptomycin-dependence mutations in ribosomal protein S12 interfere with tRNA selection by allowing conformational distortions of the decoding site that impair GTPase activation of EF-Tu during the tRNA selection process. Distortions in the decoding site are reversed by streptomycin or by a second-site suppressor mutation in 16S rRNA. These observations encourage a refinement of the current model for decoding, wherein ribosomal protein S12 and the decoding site collaborate to optimize codon recognition and substrate discrimination during the early stages of the tRNA selection process. |
format | Online Article Text |
id | pubmed-3884664 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38846642014-12-01 The central role of protein S12 in organizing the structure of the decoding site of the ribosome Demirci, Hasan Wang, Leyi Murphy, Frank V. Murphy, Eileen L. Carr, Jennifer F. Blanchard, Scott C. Jogl, Gerwald Dahlberg, Albert E. Gregory, Steven T. RNA Articles The ribosome decodes mRNA by monitoring the geometry of codon–anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallography, we have determined that conditional-lethal, streptomycin-dependence mutations in ribosomal protein S12 interfere with tRNA selection by allowing conformational distortions of the decoding site that impair GTPase activation of EF-Tu during the tRNA selection process. Distortions in the decoding site are reversed by streptomycin or by a second-site suppressor mutation in 16S rRNA. These observations encourage a refinement of the current model for decoding, wherein ribosomal protein S12 and the decoding site collaborate to optimize codon recognition and substrate discrimination during the early stages of the tRNA selection process. Cold Spring Harbor Laboratory Press 2013-12 /pmc/articles/PMC3884664/ /pubmed/24152548 http://dx.doi.org/10.1261/rna.040030.113 Text en © 2013 Demirci et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/3.0/ 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 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/. |
spellingShingle | Articles Demirci, Hasan Wang, Leyi Murphy, Frank V. Murphy, Eileen L. Carr, Jennifer F. Blanchard, Scott C. Jogl, Gerwald Dahlberg, Albert E. Gregory, Steven T. The central role of protein S12 in organizing the structure of the decoding site of the ribosome |
title | The central role of protein S12 in organizing the structure of the decoding site of the ribosome |
title_full | The central role of protein S12 in organizing the structure of the decoding site of the ribosome |
title_fullStr | The central role of protein S12 in organizing the structure of the decoding site of the ribosome |
title_full_unstemmed | The central role of protein S12 in organizing the structure of the decoding site of the ribosome |
title_short | The central role of protein S12 in organizing the structure of the decoding site of the ribosome |
title_sort | central role of protein s12 in organizing the structure of the decoding site of the ribosome |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3884664/ https://www.ncbi.nlm.nih.gov/pubmed/24152548 http://dx.doi.org/10.1261/rna.040030.113 |
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