6G04

NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119)

6G04 の概要

• エントリーDOI: 10.2210/pdb6g04/pdb
• 関連するPDBエントリー: 6G03
• NMR情報: BMRB: 34248
• 分子名称: Pre-rRNA-processing protein TSR2, 40S ribosomal protein S26-A (2 entities in total)
• 機能のキーワード: ribosome maturation, transport of ribosomal protein s26, nuclear unloading factor, escortin, nucleus, alpha-helical protein, eukaryotic specific segments, transport protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20841.37

構造登録者

Michel, E.,Schuetz, S.,Damberger, F.F.,Allain, F.H.-T.,Panse, V.G. (登録日: 2018-03-16, 公開日: 2018-09-19, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

SOLUTION NMR