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• W4280498836 abstract "Abstract Life depends on proteins, which all exist in nascent states when the growing polypeptide chain is covalently attached to a tRNA within the ribosome. Although the nascent chains; i . e ., polypeptidyl-tRNAs (pep-tRNAs), are considered as merely transient intermediates during protein synthesis, recent advances have revealed that they are directly involved in a variety of cell functions, such as gene expression control. An increasing appreciation for fine-tuning at translational levels demands a general method to handle the pep-tRNAs on a large scale. Here, we developed a method to enrich the pep-tRNAs by organic solvent extraction and silica column separation, and then identify their polypeptide moieties by mass spectrometry. As a proof-of-concept experiment using Escherichia coli , we identified ∼500 peptides derived from the pep-tRNAs, which were markedly biased towards the N-terminal regions, reflecting that the method captured the intermediate pep-tRNA population during translation. Furthermore, the method identified a subset of pep-tRNAs that were resistant to puromycin treatment, suggesting that these pep-tRNAs accumulated due to nascent-chain dependent translational pausing. Although the current specificity and comprehensiveness of the pep-tRNA enrichment have room for improvement, this new method will complement conventional methods for profiling nascent chains. Significance Statement In the central dogma of biology, RNA, an informational molecule, and protein, a functional molecule, are usually regarded as two completely independent molecular species. However, they are combined into a single species called peptidyl-tRNA (pep-tRNA) during the translation process in the ribosome. Despite the importance of pep-tRNAs as precursors of all proteins in the cell, a general method to analyze pep-tRNAs on a large scale was lacking. Taking advantage of the properties of pep-tRNAs as RNA and protein, we developed a method termed pe ptidyl- t RNA e nrichment using o rganic extraction and s ilica adsorption (PETEOS). PETEOS not only provides a unique approach to examine the nascent state of proteins but also may be effective in exploring peptides that cause translational pauses." @default.
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• W4280498836 date "2022-04-23" @default.
• W4280498836 modified "2023-10-15" @default.
• W4280498836 title "A method to enrich polypeptidyl-tRNAs to capture snapshots of translation in the cell" @default.
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• W4280498836 doi "https://doi.org/10.1101/2022.04.22.489242" @default.
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