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@ARTICLE{Minoia:288534,
      author       = {M. Minoia and J. Quintana-Cordero and K. Jetzinger$^*$ and
                      I. E. Kotan and K. J. Turnbull and M. Ciccarelli and A. E.
                      Masser and D. Liebers and E. Gouarin and M. Czech and V.
                      Hauryliuk and B. Bukau$^*$ and G. Kramer$^*$ and C.
                      Andréasson},
      title        = {{C}hp1 is a dedicated chaperone at the ribosome that
                      safeguards e{EF}1{A} biogenesis.},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DKFZ-2024-00398},
      pages        = {1382},
      year         = {2024},
      note         = {DKFZ-ZMBH Alliance},
      abstract     = {Cotranslational protein folding depends on general
                      chaperones that engage highly diverse nascent chains at the
                      ribosomes. Here we discover a dedicated ribosome-associated
                      chaperone, Chp1, that rewires the cotranslational folding
                      machinery to assist in the challenging biogenesis of
                      abundantly expressed eukaryotic translation elongation
                      factor 1A (eEF1A). Our results indicate that during eEF1A
                      synthesis, Chp1 is recruited to the ribosome with the help
                      of the nascent polypeptide-associated complex (NAC), where
                      it safeguards eEF1A biogenesis. Aberrant eEF1A production in
                      the absence of Chp1 triggers instant proteolysis, widespread
                      protein aggregation, activation of Hsf1 stress transcription
                      and compromises cellular fitness. The expression of
                      pathogenic eEF1A2 variants linked to epileptic-dyskinetic
                      encephalopathy is protected by Chp1. Thus, eEF1A is a
                      difficult-to-fold protein that necessitates a biogenesis
                      pathway starting with dedicated folding factor Chp1 at the
                      ribosome to protect the eukaryotic cell from proteostasis
                      collapse.},
      keywords     = {Ribosomes: genetics / Ribosomes: metabolism / Protein
                      Folding / Proteostasis / Eukaryotic Cells: metabolism /
                      Protein Biosynthesis},
      cin          = {A250},
      ddc          = {500},
      cid          = {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:38360885},
      pmc          = {pmc:PMC10869706},
      doi          = {10.1038/s41467-024-45645-w},
      url          = {https://inrepo02.dkfz.de/record/288534},
}