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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Vydané v:	Nature (London) Ročník 530; číslo 7590; s. 298 - 302
Hlavní autori:	Nguyen, Thi Hoang Duong, Galej, Wojciech P., Bai, Xiao-chen, Oubridge, Chris, Newman, Andrew J., Scheres, Sjors H. W., Nagai, Kiyoshi
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature Publishing Group UK 18.02.2016 Nature Publishing Group
Predmet:	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
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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. 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.
AbstractList	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. 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 Y-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. 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. 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.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.
Audience	Academic
Author	Galej, Wojciech P. Bai, Xiao-chen Oubridge, Chris Nguyen, Thi Hoang Duong Newman, Andrew J. Scheres, Sjors H. W. Nagai, Kiyoshi
Author_xml	– sequence: 1 givenname: Thi Hoang Duong surname: Nguyen fullname: Nguyen, Thi Hoang Duong email: knguyen@mrc-lmb.cam.ac.uk organization: MRC Laboratory of Molecular Biology – sequence: 2 givenname: Wojciech P. surname: Galej fullname: Galej, Wojciech P. email: wgalej@mrc-lmb.cam.ac.uk organization: MRC Laboratory of Molecular Biology – sequence: 3 givenname: Xiao-chen surname: Bai fullname: Bai, Xiao-chen organization: MRC Laboratory of Molecular Biology – sequence: 4 givenname: Chris surname: Oubridge fullname: Oubridge, Chris organization: MRC Laboratory of Molecular Biology – sequence: 5 givenname: Andrew J. surname: Newman fullname: Newman, Andrew J. organization: MRC Laboratory of Molecular Biology – sequence: 6 givenname: Sjors H. W. surname: Scheres fullname: Scheres, Sjors H. W. organization: MRC Laboratory of Molecular Biology – sequence: 7 givenname: Kiyoshi surname: Nagai fullname: Nagai, Kiyoshi email: kn@mrc-lmb.cam.ac.uk organization: MRC Laboratory of Molecular Biology
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/26829225$$D View this record in MEDLINE/PubMed
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Copyright	Springer Nature Limited 2016 COPYRIGHT 2016 Nature Publishing Group Copyright Nature Publishing Group Feb 18, 2016
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Snippet	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 represents a substantial part of the spliceosome before activation. A cryo-electron microscopy structure of Saccharomyces cerevisiae...
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SubjectTerms	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
Title	Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution
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