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-Structure paper
Title | Structure of the yeast spliceosomal postcatalytic P complex. |
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Journal, issue, pages | Science, Vol. 358, Issue 6368, Page 1278-1283, Year 2017 |
Publish date | Dec 8, 2017 |
Authors | Shiheng Liu / Xueni Li / Lingdi Zhang / Jiansen Jiang / Ryan C Hill / Yanxiang Cui / Kirk C Hansen / Z Hong Zhou / Rui Zhao / |
PubMed Abstract | 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. |
External links | Science / PubMed:29146870 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 Å |
Structure data | |
Chemicals | ChemComp-MG: ChemComp-IHP: ChemComp-GTP: ChemComp-ZN: |
Source |
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Keywords | RNA BINDING PROTEIN / pre-mRNA splicing / spliceosome / post-catalytic / P complex |