9ESI

Structure of a B-state intermediate committed to discard (Bd-II state)

9ESI の概要

• エントリーDOI: 10.2210/pdb9esi/pdb
• 関連するPDBエントリー: 9ESH
• EMDBエントリー: 19941 19942
• 分子名称: Stress response protein bis1, Small nuclear ribonucleoprotein Sm D1, Small nuclear ribonucleoprotein Sm D2, ... (45 entities in total)
• 機能のキーワード: helicase, g-patch protein, discard pathway, splicing
• 由来する生物種: Schizosaccharomyces pombe (fission yeast); 詳細
• タンパク質・核酸の鎖数: 43
• 化学式量合計: 2165647.88

構造登録者

Soni, K.,Wild, K.,Sinning, I. (登録日: 2024-03-26, 公開日: 2024-12-25, 最終更新日: 2025-05-28)

主引用文献

Soni, K.,Horvath, A.,Dybkov, O.,Schwan, M.,Trakansuebkul, S.,Flemming, D.,Wild, K.,Urlaub, H.,Fischer, T.,Sinning, I.
Structures of aberrant spliceosome intermediates on their way to disassembly.
Nat.Struct.Mol.Biol., 32:914-925, 2025

PubMed Abstract: Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans. While key steps of the canonical spliceosome cycle have been revealed by combined structure-function analyses, structural information on an aberrant spliceosome committed to premature disassembly is not available. Here, we report two cryo-electron microscopy structures of post-B spliceosome intermediates from Schizosaccharomyces pombe primed for disassembly. We identify the DEAH-box helicase-G-patch protein pair (Gih35-Gpl1, homologous to human DHX35-GPATCH1) and show how it maintains catalytic dormancy. In both structures, Gpl1 recognizes a remodeled active site introduced by an overstabilization of the U5 loop I interaction with the 5' exon leading to a single-nucleotide insertion at the 5' splice site. Remodeling is communicated to the spliceosome surface and the Ntr1 complex that mediates disassembly is recruited. Our data pave the way for a targeted analysis of splicing quality control.

PubMed: 39833470
DOI: 10.1038/s41594-024-01480-7

実験手法

ELECTRON MICROSCOPY (3.1 Å)