ArticleNature communications2018
Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Selection and Validation of Suitable Reference Genes for RT-qPCR Normalization inPlants (Basel, Switzerland) · 2026Article
- Ribosome-associated proteins in fungal ribosome homeostasis: Conceptual opportunities for peptide-based modulation.Journal of microbiology (Seoul, Korea) · 2026Review
- Article
- Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024Review
- The ubiquitin-proteasome system regulates the formation of specialized ribosomes during high salt stress in yeast.bioRxiv : the preprint server for biology · 2024Article
- Dual protection by Bcp1 and Rkm1 ensures incorporation of uL14 into pre-60S ribosomal subunits.The Journal of cell biology · 2024Article
- Chaperone-directed ribosome repair after oxidative damage.Molecular cell · 2023Article
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- The chaperone Tsr2 regulates Rps26 release and reincorporation from mature ribosomes to enable a reversible, ribosome-mediated response to stress.Science advances · 2022Article
- Slow and temperature-compensated autonomous disassembly of KaiB-KaiC complex.Biophysics and physicobiology · 2022Article
- Article
- Cryo-EM study of an archaeal 30S initiation complex gives insights into evolution of translation initiation.Communications biology · 2020Article
- Recent Advances in Archaeal Translation Initiation.Frontiers in microbiology · 2020Review
- Puf6 and Loc1 Are the Dedicated Chaperones of Ribosomal Protein Rpl43 inInternational journal of molecular sciences · 2019Article
- Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.Nucleic acids research · 2019Article
- How I manage children with Diamond-Blackfan anaemia.British journal of haematology · 2019Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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