6g04
NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119)NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119)
Structural highlights
Function[TSR2_YEAST] Required for 20S pre-rRNA processing.[1] Publication Abstract from PubMedDisordered 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. Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2.,Schutz S, Michel E, Damberger FF, Oplova M, Pena C, Leitner A, Aebersold R, Allain FH, Panse VG Nat Commun. 2018 Sep 10;9(1):3669. doi: 10.1038/s41467-018-06160-x. PMID:30201955[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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