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@ARTICLE{Wruck:303649,
      author       = {F. Wruck and J. Schmitt and K. Till and K. Fenzl and M.
                      Bertolini and F. Tippmann and A. Katranidis and B. Bukau$^*$
                      and G. Kramer and S. J. Tans},
      title        = {{C}o-translational ribosome pairing enables native assembly
                      of misfolding-prone subunits.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DKFZ-2025-01713},
      pages        = {7626},
      year         = {2025},
      note         = {A250 30.09.2023 geschlossen},
      abstract     = {Protein complexes are pivotal to most cellular processes.
                      Emerging evidence indicating dimer assembly by pairs of
                      ribosomes suggests yet unknown folding mechanisms involving
                      two nascent chains. Here, we show that co-translational
                      ribosome pairing allows their nascent chains to 'chaperone
                      each other', thus enabling the formation of coiled-coil
                      homodimers from subunits that misfold individually. We
                      developed an integrated single-molecule fluorescence and
                      force spectroscopy approach to probe the folding and
                      assembly of two nascent chains extending from nearby
                      ribosomes, using the intermediate filament lamin as a model
                      system. Ribosome proximity during early translation stages
                      is found to be critical: when interactions between nascent
                      chains are inhibited or delayed, they become trapped in
                      stable misfolded states that are no longer
                      assembly-competent. Conversely, early interactions allow the
                      two nascent chains to nucleate native-like quaternary
                      structures that grow in size and stability as translation
                      advances. We conjecture that protein folding mechanisms
                      enabled by ribosome cooperation are more broadly relevant to
                      intermediate filaments and other protein classes.},
      cin          = {Z999},
      ddc          = {500},
      cid          = {I:(DE-He78)Z999-20160331},
      pnm          = {319H - Addenda (POF4-319H)},
      pid          = {G:(DE-HGF)POF4-319H},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40817089},
      pmc          = {pmc:PMC12356879},
      doi          = {10.1038/s41467-025-61500-y},
      url          = {https://inrepo02.dkfz.de/record/303649},
}