Hoernes, Thomas Philipp; Clementi, Nina; Juen, Michael Andreas; Shi, Xinying; Faserl, Klaus; Willi, Jessica; Gasser, Catherina; Kreutz, Christoph; Joseph, Simpson; Lindner, Herbert; Hüttenhofer, Alexander; Erlacher, Matthias David (2018). Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 115(3), E382-E389. National Academy of Sciences NAS 10.1073/pnas.1714554115
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Erlacher_stop codon_PNAS 2018.pdf - Published Version Available under License Creative Commons: Attribution-Noncommercial-No Derivative Works (CC-BY-NC-ND). Download (1MB) | Preview |
Termination of protein synthesis is triggered by the recognition of a stop codon at the ribosomal A site and is mediated by class I release factors (RFs). Whereas in bacteria, RF1 and RF2 promote termination at UAA/UAG and UAA/UGA stop codons, respectively, eukaryotes only depend on one RF (eRF1) to initiate peptide release at all three stop codons. Based on several structural as well as biochemical studies, interactions between mRNA, tRNA, and rRNA have been proposed to be required for stop codon recognition. In this study, the influence of these interactions was investigated by using chemically modified stop codons. Single functional groups within stop codon nucleotides were substituted to weaken or completely eliminate specific interactions between the respective mRNA and RFs. Our findings provide detailed insight into the recognition mode of bacterial and eukaryotic RFs, thereby revealing the chemical groups of nucleotides that define the identity of stop codons and provide the means to discriminate against noncognate stop codons or UGG sense codons.
Item Type: |
Journal Article (Original Article) |
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Division/Institute: |
08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) |
Graduate School: |
Graduate School for Cellular and Biomedical Sciences (GCB) |
UniBE Contributor: |
Willi, Jessica |
Subjects: |
500 Science > 570 Life sciences; biology 500 Science > 540 Chemistry |
ISSN: |
0027-8424 |
Publisher: |
National Academy of Sciences NAS |
Language: |
English |
Submitter: |
Christina Schüpbach |
Date Deposited: |
26 Jan 2018 17:00 |
Last Modified: |
05 Dec 2022 15:09 |
Publisher DOI: |
10.1073/pnas.1714554115 |
PubMed ID: |
29298914 |
BORIS DOI: |
10.7892/boris.108769 |
URI: |
https://boris.unibe.ch/id/eprint/108769 |
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