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

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 (snRN...

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Bibliographic Details
Published in:Nature (London) Vol. 530; no. 7590; pp. 298 - 302
Main Authors: Nguyen, Thi Hoang Duong, Galej, Wojciech P., Bai, Xiao-chen, Oubridge, Chris, Newman, Andrew J., Scheres, Sjors H. W., Nagai, Kiyoshi
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 18.02.2016
Nature Publishing Group
Subjects:
631/337/1645/1792
631/45/500
631/535/1258/1259
Base Pairing
Catalytic Domain
Cryoelectron Microscopy
DNA Helicases - metabolism
Exons - genetics
Guanosine Triphosphate - metabolism
Histidine
Humanities and Social Sciences
Hydrogen Bonding
Influence
Messenger RNA
Microscopy
Models, Molecular
Molecular structure
multidisciplinary
Nucleic Acid Conformation
Physiological aspects
Polypeptides
Proteins
Ribonucleic acid
Ribonucleoprotein, U4-U6 Small Nuclear - chemistry
Ribonucleoprotein, U4-U6 Small Nuclear - metabolism
Ribonucleoprotein, U5 Small Nuclear - chemistry
Ribonucleoprotein, U5 Small Nuclear - metabolism
Ribonucleoproteins, Small Nuclear - chemistry
Ribonucleoproteins, Small Nuclear - genetics
Ribonucleoproteins, Small Nuclear - metabolism
Ribonucleoproteins, Small Nuclear - ultrastructure
RNA
RNA Splice Sites
RNA, Small Nuclear - chemistry
RNA, Small Nuclear - genetics
RNA, Small Nuclear - metabolism
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - growth & development
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Science
Spliceosomes - metabolism
Yeast
Yeast fungi
Yeasts
ISSN:0028-0836, 1476-4687, 1476-4687
Online Access:Get full text
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Summary: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. A 3.7 Å resolution structure for the yeast U4/U6.U5 tri-snRNP, a complex involved in splicing, allows a better appreciation of the architecture of the tri-snRNP, and offers new functional insights into the activation of the spliceosome and the assembly of the catalytic core. Yeast U4/U6.U5 tri-snRNP structure Following up on their 5.9 Å cryo-electron microscopy structure published less than a year ago, Kiyoshi Nagai and colleagues have now achieved a resolution of 3.7 Å for the yeast U4/U6.U5 tri-snRNP, a complex involved in splicing of messenger RNA. The improved resolution allows a better appreciation of the architecture of the tri-snRNP, and offers new functional insights into the activation of the spliceosome and the assembly of the catalytic core.
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ISSN:0028-0836
1476-4687
1476-4687
DOI:10.1038/nature16940