Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo
| Autor: | Günter Kramer, Bernd Bukau, Felix Gloge, Arzu Sandikci, Eugene Oh, Robert J. Nichols, Athanasios Typas, Carol A. Gross, Rachna Chaba, Jonathan S. Weissman, Annemarie H. Becker, Damon Huber |
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| Rok vydání: | 2011 |
| Předmět: |
Cytoplasm
Molecular Sequence Data Ribosome Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Escherichia coli Protein biosynthesis Ribosome profiling 030304 developmental biology Peptidylprolyl isomerase 0303 health sciences biology Biochemistry Genetics and Molecular Biology(all) Escherichia coli Proteins Membrane Proteins Peptidylprolyl Isomerase Transport protein Cell biology Protein Transport Biochemistry Membrane protein Protein Biosynthesis Chaperone (protein) biology.protein Bacterial outer membrane Ribosomes 030217 neurology & neurosurgery Molecular Chaperones |
| Zdroj: | Cell. 147(6):1295-1308 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/j.cell.2011.10.044 |
| Popis: | SummaryAs nascent polypeptides exit ribosomes, they are engaged by a series of processing, targeting, and folding factors. Here, we present a selective ribosome profiling strategy that enables global monitoring of when these factors engage polypeptides in the complex cellular environment. Studies of the Escherichia coli chaperone trigger factor (TF) reveal that, though TF can interact with many polypeptides, β-barrel outer-membrane proteins are the most prominent substrates. Loss of TF leads to broad outer-membrane defects and premature, cotranslational protein translocation. Whereas in vitro studies suggested that TF is prebound to ribosomes waiting for polypeptides to emerge from the exit channel, we find that in vivo TF engages ribosomes only after ∼100 amino acids are translated. Moreover, excess TF interferes with cotranslational removal of the N-terminal formyl methionine. Our studies support a triaging model in which proper protein biogenesis relies on the fine-tuned, sequential engagement of processing, targeting, and folding factors.PaperClip |
| Databáze: | OpenAIRE |
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