Lührmann, Reinhard

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[["dc.bibliographiccitation.firstpage","5528"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","5543"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Deckert, Jochen"],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Boehringer, Daniel"],["dc.contributor.author","Behzadnia, Nastaran"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2021-03-05T08:59:02Z"],["dc.date.available","2021-03-05T08:59:02Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1128/MCB.00582-06"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80332"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","Protein Composition and Electron Microscopy Structure of Affinity-Purified Human Spliceosomal B Complexes Isolated under Physiological Conditions"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","593"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","608"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Dube, Prakash"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-11-07T11:21:51Z"],["dc.date.available","2018-11-07T11:21:51Z"],["dc.date.issued","2009"],["dc.description.abstract","Metazoan spliceosomes exhibit an elaborate protein composition required for canonical and alternative splicing. Thus, the minimal set of proteins essential for activation and catalysis remains elusive. We therefore purified in vitro assembled, precatalytic spliceosomal complex B, activated Bact, and step 1 complex C from the simple eukaryote Saccharomyces cerevisiae. Mass spectrometry revealed that yeast spliceosomes contain fewer proteins than metazoans and that each functional stage is very homogeneous. Dramatic compositional changes convert B to Bact, which is composed of similar to 40 evolutionarily conserved proteins that organize the catalytic core. Additional remodeling occurs concomitant with step 1, during which nine proteins are recruited to form complex C. The moderate number of proteins recruited to complex C will allow investigations of the chemical reactions in a fully defined system. Electron microscopy reveals high-quality images of yeast spliceosomes at defined functional stages, indicating that they are well-suited for three-dimensional structure analyses."],["dc.description.sponsorship","European Commission [EURASNET-518238]; Ernst Jung Stiftung"],["dc.identifier.doi","10.1016/j.molcel.2009.09.040"],["dc.identifier.isi","000272534800008"],["dc.identifier.pmid","19941820"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55879"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-2765"],["dc.title","The Evolutionarily Conserved Core Design of the Catalytic Activation Step of the Yeast Spliceosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","463"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","468"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Boehringer, Daniel"],["dc.contributor.author","Makarov, Evgeny M."],["dc.contributor.author","Sander, Bjoern"],["dc.contributor.author","Makarova, Olga V."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2021-03-05T08:58:30Z"],["dc.date.available","2021-03-05T08:58:30Z"],["dc.date.issued","2004"],["dc.identifier.doi","10.1038/nsmb761"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80158"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.title","Three-dimensional structure of a pre-catalytic human spliceosomal complex B"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","53"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","55"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Golas, Monika Mariola"],["dc.contributor.author","Sander, Bjoern"],["dc.contributor.author","Dube, Prakash"],["dc.contributor.author","Boehringer, Daniel"],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Deckert, Jochen"],["dc.contributor.author","Hauer, Florian"],["dc.contributor.author","Wolf, Elmar"],["dc.contributor.author","Uchtenhagen, Hannes"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Herzog, Franz"],["dc.contributor.author","Peters, Jan Michael"],["dc.contributor.author","Poerschke, Dietmar"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2021-03-05T08:58:29Z"],["dc.date.available","2021-03-05T08:58:29Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1038/nmeth1139"],["dc.identifier.pii","BFnmeth1139"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80155"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.title","GraFix: sample preparation for single-particle electron cryomicroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","318"],["dc.bibliographiccitation.issue","7641"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.volume","542"],["dc.contributor.author","Bertram, Karl"],["dc.contributor.author","Agafonov, Dmitry E."],["dc.contributor.author","Liu, Wen-Ti"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-11-07T10:27:23Z"],["dc.date.available","2018-11-07T10:27:23Z"],["dc.date.issued","2017"],["dc.description.abstract","Spliceosome rearrangements facilitated by RNA helicase PRP16 before catalytic step two of splicing are poorly understood. Here we report a 3D cryo-electron microscopy structure of the human spliceosomal C complex stalled directly after PRP16 action (C ). The architecture of the catalytic U2-U6 ribonucleoprotein (RNP) core of the human C spliceosome is very similar to that of the yeast pre-Prp16 C complex. However, in C the branched intron region is separated from the catalytic centre by approximately 20 angstrom, and its position close to the U6 small nuclear RNA ACAGA box is stabilized by interactions with the PRP8 RNase H-like and PRP17 WD40 domains. RNA helicase PRP22 is located about 100 angstrom from the catalytic centre, suggesting that it destabilizes the spliced mRNA after step two from a distance. Comparison of the structure of the yeast C and human C complexes reveals numerous RNP rearrangements that are likely to be facilitated by PRP16, including a large-scale movement of the U2 small nuclear RNP."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 860]"],["dc.identifier.doi","10.1038/nature21079"],["dc.identifier.isi","000394451600030"],["dc.identifier.pmid","28076346"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43225"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","Cryo-EM structure of a human spliceosome activated for step 2 of splicing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2528"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","2537"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Karaduman, Ramazan"],["dc.contributor.author","Dube, Prakash"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-11-07T11:08:52Z"],["dc.date.available","2018-11-07T11:08:52Z"],["dc.date.issued","2008"],["dc.description.abstract","Protein components of the U6 snRNP (Prp24p and LSm2-8) are thought to act cooperatively in facilitating the annealing of U6 and U4 snRNAs during U4/U6 di-snRNP formation. To learn more about the spatial arrangement of these proteins in S. cerevisiae U6 snRNPs, we investigated the structure of this particle by electron microscopy. U6 snRNPs, purified by affinity chromatography and gradient centrifugation, and then immediately adsorbed to the carbon film support, revealed an open form in which the Prp24 protein and the ring formed by the LSm proteins were visible as two separate morphological domains, while particles stabilized by chemical cross-linking in solution under mild conditions before binding to the carbon film exhibited a compact form, with the two domains in close proximity to one another. In the open form, individual LSm proteins were located by a novel approach employing C-terminal genetic tagging of the LSm proteins with yECitrine. These studies show the Prp24 protein at defined distances from each subunit of the LSm ring, which in turn suggests that the LSm ring is positioned in a consistent manner on the U6 RNA. Furthermore, in agreement with the EM observations, UV cross-linking revealed U6 RNA in contact with the LSm2 protein at the interface between Prp24p and the LSm ring. Further, LSmp-Prp24p interactions may be restricted to the closed form, which appears to represent the solution structure of the U6 snRNP particle."],["dc.identifier.doi","10.1261/rna.1369808"],["dc.identifier.isi","000261398400010"],["dc.identifier.pmid","18971323"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52888"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1355-8382"],["dc.title","Structure of yeast U6 snRNPs: Arrangement of Prp24p and the LSm complex as revealed by electron microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2283"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2292"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Wolf, Elmar"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Deckert, Jochen"],["dc.contributor.author","Merz, Christian"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2021-03-05T08:58:27Z"],["dc.date.available","2021-03-05T08:58:27Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1038/emboj.2009.171"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80139"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Exon, intron and splice site locations in the spliceosomal B complex"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1206"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","1212"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Häcker, Irina"],["dc.contributor.author","Sander, Bjoern"],["dc.contributor.author","Golas, Monika M."],["dc.contributor.author","Wolf, Elmar"],["dc.contributor.author","Karagöz, Elif"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-11-07T11:09:41Z"],["dc.date.available","2018-11-07T11:09:41Z"],["dc.date.issued","2008"],["dc.description.abstract","The U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP) is a major, evolutionarily highly conserved spliceosome subunit. Unwinding of its U4/U6 snRNA duplex is a central event of spliceosome activation that requires several components of the U5 portion of the tri-snRNP, including the RNA helicase Brr2, Prp8 and the GTPase Snu114. Here we report the EM projection structure of the Saccharomyces cerevisiae tri-snRNP. It shows a modular organization comprising three extruding domains that contact one another in its central portion. We have visualized genetically tagged tri-snRNP proteins by EM and show here that U4/U6 snRNP forms a domain termed the arm. Conversely, a separate head domain adjacent to the arm harbors Brr2, whereas Prp8 and the GTPase Snu114 are located centrally. The head and arm adopt variable relative positions. This molecular organization and dynamics suggest possible scenarios for structural events during catalytic activation."],["dc.identifier.doi","10.1038/nsmb.1506"],["dc.identifier.isi","000260638500019"],["dc.identifier.pmid","18953335"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53061"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","1545-9985"],["dc.title","Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","454"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","464.e11"],["dc.bibliographiccitation.volume","172"],["dc.contributor.author","Haselbach, David"],["dc.contributor.author","Komarov, Ilya"],["dc.contributor.author","Agafonov, Dmitry E."],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Graf, Benjamin"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2020-12-10T14:22:58Z"],["dc.date.available","2020-12-10T14:22:58Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.cell.2018.01.010"],["dc.identifier.issn","0092-8674"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71792"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]