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Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2

Author

Listed:
  • Sabina Schütz

    (University of Zurich)

  • Erich Michel

    (University of Zurich)

  • Fred F. Damberger

    (ETH Zurich)

  • Michaela Oplová

    (University of Zurich
    ETH Zurich)

  • Cohue Peña

    (University of Zurich)

  • Alexander Leitner

    (ETH Zurich)

  • Ruedi Aebersold

    (ETH Zurich
    University of Zurich)

  • Frederic H.-T. Allain

    (ETH Zurich)

  • Vikram Govind Panse

    (University of Zurich)

Abstract

Disordered extensions at the termini and short internal insertions distinguish eukaryotic ribosomal proteins (r-proteins) from their anucleated archaeal counterparts. Here, we report an NMR structure of such a eukaryotic-specific segment (ESS) in the r-protein eS26 in complex with the escortin Tsr2. The structure reveals how ESS attracts Tsr2 specifically to importin:eS26 complexes entering the nucleus in order to trigger non-canonical RanGTP-independent disassembly. Tsr2 then sequesters the released eS26 and prevents rebinding to the importin, providing an alternative allosteric mechanism to terminate the process of nuclear import. Notably, a Diamond–Blackfan anemia-associated Tsr2 mutant protein is impaired in binding to ESS, unveiling a critical role for this interaction in human hematopoiesis. We propose that eS26-ESS and Tsr2 are components of a nuclear sorting system that co-evolved with the emergence of the nucleocytoplasmic barrier and transport carriers.

Suggested Citation

  • Sabina Schütz & Erich Michel & Fred F. Damberger & Michaela Oplová & Cohue Peña & Alexander Leitner & Ruedi Aebersold & Frederic H.-T. Allain & Vikram Govind Panse, 2018. "Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06160-x
    DOI: 10.1038/s41467-018-06160-x
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