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Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Hoernes Thomas, Clementi Nina, Juen Michael, Shi Xinying, Faserl Klaus, Willi Jessica, Gasser Catherina, Kreutz Christoph, Joseph Simpson, Lindner Herbert, Hüttenhofer Alexander, Erlacher Matthias,
Project Stress-mediated effects on ribosome functions and translation control
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Original article (peer-reviewed)

Journal Proceedings of the National Academy of Sciences
Page(s) E382
Title of proceedings Proceedings of the National Academy of Sciences
DOI 10.1073/pnas

Open Access

URL https://www.pnas.org/content/115/3/E382.long
Type of Open Access Publisher (Gold Open Access)

Abstract

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.
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