6G03

NMR Solution Structure of yeast TSR2(1-152)

Summary for 6G03

• Entry DOI: 10.2210/pdb6g03/pdb
• NMR Information: BMRB: 34247
• Descriptor: Pre-rRNA-processing protein TSR2 (1 entity in total)
• Functional Keywords: ribosome maturation, transport of ribosomal protein s26, nuclear unloading factor, escortin, nucleus, alpha-helical protein, eukaryotic specific segments, transport protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 17938.06

Authors

Michel, E.,Schuetz, S.,Damberger, F.F.,Allain, F.H.-T.,Panse, V.G. (deposition date: 2018-03-16, release date: 2018-09-19, Last modification date: 2024-06-19)

Primary citation

Schutz, S.,Michel, E.,Damberger, F.F.,Oplova, M.,Pena, C.,Leitner, A.,Aebersold, R.,Allain, F.H.,Panse, V.G.
Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2.
Nat Commun, 9:3669-3669, 2018

PubMed 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.

PubMed: 30201955
DOI: 10.1038/s41467-018-06160-x

Experimental method

SOLUTION NMR