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| 001 | 303193 | ||
| 005 | 20250819100257.0 | ||
| 024 | 7 | _ | |a 10.1073/pnas.2422678122 |2 doi |
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| 024 | 7 | _ | |a 0027-8424 |2 ISSN |
| 024 | 7 | _ | |a 1091-6490 |2 ISSN |
| 037 | _ | _ | |a DKFZ-2025-01544 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 500 |
| 100 | 1 | _ | |a Till, Katharina |b 0 |
| 245 | _ | _ | |a Trigger factor accelerates nascent chain compaction and folding. |
| 260 | _ | _ | |a Washington, DC |c 2025 |b National Acad. of Sciences |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1755590553_6401 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a Conformational control of nascent chains is poorly understood. Chaperones are known to stabilize, unfold, and disaggregate polypeptides away from the ribosome. In comparison, much less is known about the elementary conformational control mechanisms at the ribosome. Yet, proteins encounter major folding and aggregation challenges during translation. Here, using selective ribosome profiling and optical tweezers with correlated single-molecule fluorescence, with dihydrofolate reductase (DHFR) as a model system, we show that the Escherichia coli chaperone trigger factor (TF) accelerates nascent chain folding. TF scans nascent chains by transient binding events, and then locks into a stable binding mode as the chain collapses and folds. This interplay is reciprocal: TF binding collapses nascent chains and stabilizes partial folds, while nascent chain compaction prolongs TF binding. Ongoing translation controls these cooperative effects, with TF-accelerated folding depending on the emergence of a peptide segment that is central to the core DHFR beta-sheet. The folding acceleration we report here impacts processes that depend on folding occurring cotranslationally, including cotranslational protein assembly, protein aggregation, and translational pausing, and may be relevant to other domains of life. |
| 536 | _ | _ | |a 311 - Zellbiologie und Tumorbiologie (POF4-311) |0 G:(DE-HGF)POF4-311 |c POF4-311 |f POF IV |x 0 |
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| 650 | _ | 7 | |a chaperones |2 Other |
| 650 | _ | 7 | |a optical tweezers |2 Other |
| 650 | _ | 7 | |a protein folding |2 Other |
| 650 | _ | 7 | |a ribosomes |2 Other |
| 650 | _ | 7 | |a Escherichia coli Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Tetrahydrofolate Dehydrogenase |0 EC 1.5.1.3 |2 NLM Chemicals |
| 650 | _ | 7 | |a trigger factor, E coli |0 EC 5.2.1.- |2 NLM Chemicals |
| 650 | _ | 7 | |a Peptidylprolyl Isomerase |0 EC 5.2.1.8 |2 NLM Chemicals |
| 650 | _ | 7 | |a Molecular Chaperones |2 NLM Chemicals |
| 650 | _ | 2 | |a Protein Folding |2 MeSH |
| 650 | _ | 2 | |a Escherichia coli Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Escherichia coli Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a Tetrahydrofolate Dehydrogenase: metabolism |2 MeSH |
| 650 | _ | 2 | |a Tetrahydrofolate Dehydrogenase: chemistry |2 MeSH |
| 650 | _ | 2 | |a Escherichia coli: metabolism |2 MeSH |
| 650 | _ | 2 | |a Ribosomes: metabolism |2 MeSH |
| 650 | _ | 2 | |a Peptidylprolyl Isomerase: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Molecular Chaperones: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Binding |2 MeSH |
| 700 | 1 | _ | |a Seinen, Anne-Bart |0 0000-0003-4644-7732 |b 1 |
| 700 | 1 | _ | |a Wruck, Florian |b 2 |
| 700 | 1 | _ | |a Sunderlikova, Vanda |b 3 |
| 700 | 1 | _ | |a Galmozzi, Carla |0 P:(DE-He78)379b02b83ca85bcfe4c4aecf5e8c6272 |b 4 |
| 700 | 1 | _ | |a Katranidis, Alexandros |0 0000-0002-1785-1659 |b 5 |
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| 700 | 1 | _ | |a Kramer, Günter |0 P:(DE-He78)8b9aa336210db1592efa7400628e5a46 |b 7 |
| 700 | 1 | _ | |a Tans, Sander J |0 0000-0002-7131-2568 |b 8 |
| 773 | _ | _ | |a 10.1073/pnas.2422678122 |g Vol. 122, no. 30, p. e2422678122 |0 PERI:(DE-600)1461794-8 |n 30 |p e2422678122 |t Proceedings of the National Academy of Sciences of the United States of America |v 122 |y 2025 |x 0027-8424 |
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