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Structure of the yeast spliceosomal postcatalytic P complex.

ABSTRACT: The spliceosome undergoes dramatic changes in a splicing cycle. Structures of B, Bact, 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.

SUBMITTER: Liu S 

PROVIDER: S-EPMC5828012 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Structure of the yeast spliceosomal postcatalytic P complex.

Liu Shiheng S   Li Xueni X   Zhang Lingdi L   Jiang Jiansen J   Hill Ryan C RC   Cui Yanxiang Y   Hansen Kirk C KC   Zhou Z Hong ZH   Zhao Rui R  

Science (New York, N.Y.) 20171116 6368

The spliceosome undergoes dramatic changes in a splicing cycle. Structures of B, B<sup>act</sup>, 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 pai  ...[more]

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