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

Sabina Schütz, Erich Michel, Fred F. Damberger, Michaela Oplová, Cohue Peña, Alexander Leitner, Ruedi Aebersold, Frederic H.-T. Allain () and Vikram Govind Panse ()
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Sabina Schütz: University of Zurich
Erich Michel: University of Zurich
Fred F. Damberger: ETH Zurich
Michaela Oplová: University of Zurich
Cohue Peña: University of Zurich
Alexander Leitner: ETH Zurich
Ruedi Aebersold: ETH Zurich
Frederic H.-T. Allain: ETH Zurich
Vikram Govind Panse: University of Zurich

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-06160-x

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