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

Thi Hoang Duong Nguyen (), Wojciech P. Galej (), Xiao-chen Bai, Chris Oubridge, Andrew J. Newman, Sjors H. W. Scheres and Kiyoshi Nagai ()
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Thi Hoang Duong Nguyen: MRC Laboratory of Molecular Biology
Wojciech P. Galej: MRC Laboratory of Molecular Biology
Xiao-chen Bai: MRC Laboratory of Molecular Biology
Chris Oubridge: MRC Laboratory of Molecular Biology
Andrew J. Newman: MRC Laboratory of Molecular Biology
Sjors H. W. Scheres: MRC Laboratory of Molecular Biology
Kiyoshi Nagai: MRC Laboratory of Molecular Biology

Nature, 2016, vol. 530, issue 7590, 298-302

Abstract: 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.

Date: 2016
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DOI: 10.1038/nature16940

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