og:image: http://www.pnas.org/sites/default/files/highwire/pnas/115/12.cover-source.jpg citation_mjid: pnas;115/12/3018 article:published_time: 2018-03-20 og:site_name: PNAS citation_reference: citation_journal_abbrev=Adv Protein Chem Struct Biol;citation_author=SS. Yadavalli;citation_author=M. Ibba;citation_title=Quality control in aminoacyl-tRNA synthesis its role in translational fidelity.;citation_pages=1-43;citation_volume=86;citation_year=2012;citation_pmid=22243580;citation_doi=10.1016/B978-0-12-386497-0.00001-3 citation_journal_title: Proceedings of the National Academy of Sciences type: article og:description: Protein translation is a key cellular process in which each codon of mRNAs has to be accurately and efficiently recognized by cognate tRNAs of a large repertoire of noncognate tRNAs. A successful decoding process is largely dependent on the presence of modified nucleotides within the anticodon loop, especially of tRNAs having to read A/U-rich codons. In this latter case, their roles appear to stabilize the codon?anticodon interaction, allowing them to reach an optimal energetic value close to that of other interacting tRNAs involving G/C-rich anticodons. In this work we demonstrate that, while helping an efficient translation of A/U-rich codons, modified nucleotides also allow certain unconventional base pairing to occur, as evidenced in the case of stop codon suppression. citation_author_email: olivier.namy@i2bc.paris-saclay.fr citation_issn: 0027-8424 citation_full_html_url: http://www.pnas.org/content/115/12/3018.full citation_public_url: http://www.pnas.org/content/115/12/3018 dc:title: Deciphering the reading of the genetic code by near-cognate tRNA | PNAS Content-Encoding: UTF-8 citation_pdf_url: http://www.pnas.org/content/115/12/3018.full.pdf citation_section: Biological Sciences citation_num_pages: 6 citation_lastpage: 3023 citation_fulltext_world_readable: citation_journal_abbrev: PNAS DC.Identifier: 10.1073/pnas.1715578115 DC.Rights: Copyright © 2018 the Author(s). Published by PNAS.. This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND). citation_author: Sandra Blanchet citation_abstract_html_url: http://www.pnas.org/content/115/12/3018.abstract citation_issue: 12 HW.identifier: /pnas/115/12/3018.atom citation_doi: 10.1073/pnas.1715578115 citation_volume: 115 Content-Language: en format-detection: telephone=no Generator: Drupal 7 (http://drupal.org) citation_author_orcid: http://orcid.org/0000-0002-1143-5961 DC.AccessRights: open-access citation_publication_date: 2018/03/20 citation_title: Deciphering the reading of the genetic code by near-cognate tRNA citation_author_institution: Université Paris-Saclay citation_publisher: National Academy of Sciences citation_id: 115/12/3018 title: Deciphering the reading of the genetic code by near-cognate tRNA | PNAS DC.Description: Protein translation is a key cellular process in which each codon of mRNAs has to be accurately and efficiently recognized by cognate tRNAs of a large repertoire of noncognate tRNAs. A successful decoding process is largely dependent on the presence of modified nucleotides within the anticodon loop, especially of tRNAs having to read A/U-rich codons. In this latter case, their roles appear to stabilize the codon?anticodon interaction, allowing them to reach an optimal energetic value close to that of other interacting tRNAs involving G/C-rich anticodons. In this work we demonstrate that, while helping an efficient translation of A/U-rich codons, modified nucleotides also allow certain unconventional base pairing to occur, as evidenced in the case of stop codon suppression. Content-Type-Hint: text/html; charset=utf-8 DC.Format: text/html DC.Publisher: National Academy of Sciences DC.Contributor: Sandra Blanchet Content-Type: application/xhtml+xml; charset=UTF-8 X-Parsed-By: org.apache.tika.parser.DefaultParser og:type: article article:section: Biological Sciences citation_pmid: 29507244 citation_article_type: Research Article og:title: Deciphering the reading of the genetic code by near-cognate tRNA citation_abstract:

Some codons of the genetic code can be read not only by cognate, but also by near-cognate tRNAs. This flexibility is thought to be conferred mainly by a mismatch between the third base of the codon and the first of the anticodon (the so-called ?wobble? position). However, this simplistic explanation underestimates the importance of nucleotide modifications in the decoding process. Using a system in which only near-cognate tRNAs can decode a specific codon, we investigated the role of six modifications of the anticodon, or adjacent nucleotides, of the tRNAs specific for Tyr, Gln, Lys, Trp, Cys, and Arg in Saccharomyces cerevisiae. Modifications almost systematically rendered these tRNAs able to act as near-cognate tRNAs at stop codons, even though they involve noncanonical base pairs, without markedly affecting their ability to decode cognate or near-cognate sense codons. These findings reveal an important effect of modifications to tRNA decoding with implications for understanding the flexibility of the genetic code.

DC.Title: Deciphering the reading of the genetic code by near-cognate tRNA issue_cover_image: http://www.pnas.org/sites/default/files/highwire/pnas/115/12.cover-source.jpg citation_firstpage: 3018 citation_funding_source: citation_funder_id=501100004099;citation_grant_number=3FI10167LVCY; HW.pisa: pnas;115/12/3018 viewport: initial-scale=1, maximum-scale=1, width=device-width, user-scalable=yes DC.Language: en DC.Date: 2018-03-20 citation_access: all category: research-article og:url: http://www.pnas.org/content/115/12/3018