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@ARTICLE{Galmozzi:301282,
      author       = {C. V. Galmozzi and F. Tippmann and F. Wruck and J. J.
                      Auburger and I. Kats$^*$ and M. Guennigmann and K. Till and
                      E. P. O Brien and S. J. Tans and G. Kramer and B. Bukau$^*$},
      title        = {{P}roteome-wide determinants of co-translational chaperone
                      binding in bacteria.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DKFZ-2025-00967},
      pages        = {4361},
      year         = {2025},
      note         = {DKFZ-ZMBH Alliance / #LA:Z999#},
      abstract     = {Chaperones are essential to the co-translational folding of
                      most proteins. However, the principles of co-translational
                      chaperone interaction throughout the proteome are poorly
                      understood, as current methods are restricted to few
                      substrates and cannot capture nascent protein folding or
                      chaperone binding sites, precluding a comprehensive
                      understanding of productive and erroneous protein
                      biosynthesis. Here, by integrating genome-wide selective
                      ribosome profiling, single-molecule tools, and computational
                      predictions using AlphaFold we show that the binding of the
                      main E. coli chaperones involved in co-translational
                      folding, Trigger Factor (TF) and DnaK correlates with
                      'unsatisfied residues' exposed on nascent partial folds -
                      residues that have begun to form tertiary structure but
                      cannot yet form all native contacts due to ongoing
                      translation. This general principle allows us to predict
                      their co-translational binding across the proteome based on
                      sequence only, which we verify experimentally. The results
                      show that TF and DnaK stably bind partially folded rather
                      than unfolded conformers. They also indicate a synergistic
                      action of TF guiding intra-domain folding and DnaK
                      preventing premature inter-domain contacts, and reveal
                      robustness in the larger chaperone network (TF, DnaK,
                      GroEL). Given the complexity of translation, folding, and
                      chaperone functions, our predictions based on general
                      chaperone binding rules indicate an unexpected underlying
                      simplicity.},
      keywords     = {Escherichia coli Proteins: metabolism / Escherichia coli
                      Proteins: genetics / Escherichia coli Proteins: chemistry /
                      Proteome: metabolism / Proteome: genetics / Escherichia
                      coli: metabolism / Escherichia coli: genetics / Protein
                      Folding / HSP70 Heat-Shock Proteins: metabolism / HSP70
                      Heat-Shock Proteins: genetics / HSP70 Heat-Shock Proteins:
                      chemistry / Protein Binding / Molecular Chaperones:
                      metabolism / Molecular Chaperones: genetics / Protein
                      Biosynthesis / Ribosomes: metabolism / Peptidylprolyl
                      Isomerase: metabolism / Peptidylprolyl Isomerase: genetics /
                      Binding Sites / Escherichia coli Proteins (NLM Chemicals) /
                      Proteome (NLM Chemicals) / dnaK protein, E coli (NLM
                      Chemicals) / trigger factor, E coli (NLM Chemicals) / HSP70
                      Heat-Shock Proteins (NLM Chemicals) / Molecular Chaperones
                      (NLM Chemicals) / Peptidylprolyl Isomerase (NLM Chemicals)},
      cin          = {B260},
      ddc          = {500},
      cid          = {I:(DE-He78)B260-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40348781},
      doi          = {10.1038/s41467-025-59067-9},
      url          = {https://inrepo02.dkfz.de/record/301282},
}