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@ARTICLE{Till:303193,
      author       = {K. Till and A.-B. Seinen and F. Wruck and V. Sunderlikova
                      and C. Galmozzi$^*$ and A. Katranidis and B. Bukau$^*$ and
                      G. Kramer$^*$ and S. J. Tans},
      title        = {{T}rigger factor accelerates nascent chain compaction and
                      folding.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {122},
      number       = {30},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DKFZ-2025-01544},
      pages        = {e2422678122},
      year         = {2025},
      note         = {DKFZ-ZMBH Alliance},
      abstract     = {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.},
      keywords     = {Protein Folding / Escherichia coli Proteins: metabolism /
                      Escherichia coli Proteins: chemistry / Tetrahydrofolate
                      Dehydrogenase: metabolism / Tetrahydrofolate Dehydrogenase:
                      chemistry / Escherichia coli: metabolism / Ribosomes:
                      metabolism / Peptidylprolyl Isomerase: metabolism / Protein
                      Biosynthesis / Molecular Chaperones: metabolism / Protein
                      Binding / chaperones (Other) / optical tweezers (Other) /
                      protein folding (Other) / ribosomes (Other) / Escherichia
                      coli Proteins (NLM Chemicals) / Tetrahydrofolate
                      Dehydrogenase (NLM Chemicals) / trigger factor, E coli (NLM
                      Chemicals) / Peptidylprolyl Isomerase (NLM Chemicals) /
                      Molecular Chaperones (NLM Chemicals)},
      cin          = {Z999 / A250},
      ddc          = {500},
      cid          = {I:(DE-He78)Z999-20160331 / I:(DE-He78)A250-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40711920},
      doi          = {10.1073/pnas.2422678122},
      url          = {https://inrepo02.dkfz.de/record/303193},
}