+検索条件
-Structure paper
タイトル | Structure of the yeast spliceosomal postcatalytic P complex. |
---|---|
ジャーナル・号・ページ | Science, Vol. 358, Issue 6368, Page 1278-1283, Year 2017 |
掲載日 | 2017年12月8日 |
著者 | Shiheng Liu / Xueni Li / Lingdi Zhang / Jiansen Jiang / Ryan C Hill / Yanxiang Cui / Kirk C Hansen / Z Hong Zhou / Rui Zhao / |
PubMed 要旨 | The spliceosome undergoes dramatic changes in a splicing cycle. Structures of B, B, C, C*, and intron lariat spliceosome complexes revealed mechanisms of 5'-splice site (ss) recognition, branching, ...The spliceosome undergoes dramatic changes in a splicing cycle. Structures of B, B, C, C*, and intron lariat spliceosome complexes revealed mechanisms of 5'-splice site (ss) recognition, branching, and intron release, but lacked information on 3'-ss recognition, exon ligation, and exon release. Here we report a cryo-electron microscopy structure of the postcatalytic P complex at 3.3-angstrom resolution, revealing that the 3' ss is mainly recognized through non-Watson-Crick base pairing with the 5' ss and branch point. Furthermore, one or more unidentified proteins become stably associated with the P complex, securing the 3' exon and potentially regulating activity of the helicase Prp22. Prp22 binds nucleotides 15 to 21 in the 3' exon, enabling it to pull the intron-exon or ligated exons in a 3' to 5' direction to achieve 3'-ss proofreading or exon release, respectively. |
リンク | Science / PubMed:29146870 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 Å |
構造データ | |
化合物 | ChemComp-MG: ChemComp-IHP: ChemComp-GTP: ChemComp-ZN: |
由来 |
|
キーワード | RNA BINDING PROTEIN / pre-mRNA splicing / spliceosome / post-catalytic / P complex |