期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 115, 期 3, 页码 E382-E389出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1714554115
关键词
ribosome; translation; peptide release; release factor; mRNA modification
资金
- Austrian Science Fund [P 22658-B12, P 28494-BBL, SFB F4411]
- European Molecular Biology Organization Short-Term Fellowship [ASTF 553-2016]
- Swiss National Science Foundation [31003A_166527]
- Austrian Science Fund (FWF) [P28494] Funding Source: Austrian Science Fund (FWF)
- Swiss National Science Foundation (SNF) [31003A_166527] Funding Source: Swiss National Science Foundation (SNF)
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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