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Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution.

<div class='caption-title'>Three orthogonal views of a near-complete atomic model of the Saccharomyces cerevisiae U4/U6.U5 tri-snRNP</div>
<div class='caption-title'>Prp8 and U4/U6 and U5 snRNAs</div>
<div class='caption-title'>Snu114 and its interaction with Prp8 and U5 snRNA</div>
Nguyen THD, Galej WP, Bai XC, Oubridge C, Newman AJ, Scheres SHW, Nagai K
OpenAccess logo Nature 530 298-302 (2016)
Related entries: 5gam, 5gao, 5gap

Cited: 136 times
EuropePMC logo PMID: 26829225

Abstract

U4/U6.U5 tri-snRNP represents a substantial part of the spliceosome before activation. A cryo-electron microscopy structure of Saccharomyces cerevisiae U4/U6.U5 tri-snRNP at 3.7 Å resolution led to an essentially complete atomic model comprising 30 proteins plus U4/U6 and U5 small nuclear RNAs (snRNAs). The structure reveals striking interweaving interactions of the protein and RNA components, including extended polypeptides penetrating into subunit interfaces. The invariant ACAGAGA sequence of U6 snRNA, which base-pairs with the 5'-splice site during catalytic activation, forms a hairpin stabilized by Dib1 and Prp8 while the adjacent nucleotides interact with the exon binding loop 1 of U5 snRNA. Snu114 harbours GTP, but its putative catalytic histidine is held away from the γ-phosphate by hydrogen bonding to a tyrosine in the amino-terminal domain of Prp8. Mutation of this histidine to alanine has no detectable effect on yeast growth. The structure provides important new insights into the spliceosome activation process leading to the formation of the catalytic centre.

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