Structure of a pre-catalytic spliceosome

Clemens Plaschka (), Pei-Chun Lin () and Kiyoshi Nagai ()
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Clemens Plaschka: MRC Laboratory of Molecular Biology
Pei-Chun Lin: MRC Laboratory of Molecular Biology
Kiyoshi Nagai: MRC Laboratory of Molecular Biology

Nature, 2017, vol. 546, issue 7660, 617-621

Abstract: Abstract Intron removal requires assembly of the spliceosome on precursor mRNA (pre-mRNA) and extensive remodelling to form the spliceosome’s catalytic centre. Here we report the cryo-electron microscopy structure of the yeast Saccharomyces cerevisiae pre-catalytic B complex spliceosome at near-atomic resolution. The mobile U2 small nuclear ribonucleoprotein particle (snRNP) associates with U4/U6.U5 tri-snRNP through the U2/U6 helix II and an interface between U4/U6 di-snRNP and the U2 snRNP SF3b-containing domain, which also transiently contacts the helicase Brr2. The 3′ region of the U2 snRNP is flexibly attached to the SF3b-containing domain and protrudes over the concave surface of tri-snRNP, where the U1 snRNP may reside before its release from the pre-mRNA 5′ splice site. The U6 ACAGAGA sequence forms a hairpin that weakly tethers the 5′ splice site. The B complex proteins Prp38, Snu23 and Spp381 bind the Prp8 N-terminal domain and stabilize U6 ACAGAGA stem–pre-mRNA and Brr2–U4 small nuclear RNA interactions. These results provide important insights into the events leading to active site formation.

Date: 2017
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DOI: 10.1038/nature22799

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