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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Veröffentlicht in:	Nature (London) Jg. 530; H. 7590; S. 298 - 302
Hauptverfasser:	Nguyen, Thi Hoang Duong, Galej, Wojciech P., Bai, Xiao-chen, Oubridge, Chris, Newman, Andrew J., Scheres, Sjors H. W., Nagai, Kiyoshi
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	London Nature Publishing Group UK 18.02.2016 Nature Publishing Group
Schlagworte:	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-Zugang:	Volltext
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Zusammenfassung:	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.
Bibliographie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	0028-0836 1476-4687 1476-4687
DOI:	10.1038/nature16940