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- Title
Quality control of protein synthesis in the early elongation stage.
- Authors
Nagao, Asuteka; Nakanishi, Yui; Yamaguchi, Yutaro; Mishina, Yoshifumi; Karoji, Minami; Toya, Takafumi; Fujita, Tomoya; Iwasaki, Shintaro; Miyauchi, Kenjyo; Sakaguchi, Yuriko; Suzuki, Tsutomu
- Abstract
In the early stage of bacterial translation, peptidyl-tRNAs frequently dissociate from the ribosome (pep-tRNA drop-off) and are recycled by peptidyl-tRNA hydrolase. Here, we establish a highly sensitive method for profiling of pep-tRNAs using mass spectrometry, and successfully detect a large number of nascent peptides from pep-tRNAs accumulated in Escherichia coli pthts strain. Based on molecular mass analysis, we found about 20% of the peptides bear single amino-acid substitutions of the N-terminal sequences of E. coli ORFs. Detailed analysis of individual pep-tRNAs and reporter assay revealed that most of the substitutions take place at the C-terminal drop-off site and that the miscoded pep-tRNAs rarely participate in the next round of elongation but dissociate from the ribosome. These findings suggest that pep-tRNA drop-off is an active mechanism by which the ribosome rejects miscoded pep-tRNAs in the early elongation, thereby contributing to quality control of protein synthesis after peptide bond formation. Peptidyl-tRNAs (pep-tRNAs) frequently dissociate from ribosome, called as pep-tRNA drop-off. But, its function remained unclear. The authors proposed a new quality control mechanism of protein synthesis by active rejection of miscoded pep-tRNAs in the early stage of translation.
- Subjects
PROTEIN synthesis; QUALITY control; TRANSFER RNA; ESCHERICHIA coli; PEPTIDE synthesis; PEPTIDE bonds
- Publication
Nature Communications, 2023, Vol 14, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-023-38077-5