Lührmann, Reinhard

[["dc.bibliographiccitation.firstpage","11440"],["dc.bibliographiccitation.issue","31"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","11445"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Donnert, Gerald"],["dc.contributor.author","Keller, Jan"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Andrei, M. Alexandra"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:52:39Z"],["dc.date.available","2017-09-07T11:52:39Z"],["dc.date.issued","2006"],["dc.description.abstract","We demonstrate far-field fluorescence microscopy with a focal-plane resolution of 15-20 nm in biological samples. The 10- to 12-fold multilateral increase in resolution below the diffraction barrier has been enabled by the elimination of molecular triplet state excitation as a major source of photobleaching of a number of dyes in stimulated emission depletion microscopy. Allowing for relaxation of the triplet state between subsequent excitation-depletion cycles yields an up to 30-fold increase in total fluorescence signal as compared with reported stimulated emission depletion illumination schemes. Moreover, it enables the reduction of the effective focal spot area by up to approximate to 140-fold below that given by diffraction. Triplet-state relaxation can be realized either by reducing the repetition rate of pulsed lasers or by increasing the scanning speed such that the build-up of the triplet state is effectively prevented. This resolution in immunofluorescence imaging is evidenced by revealing nanoscale protein patterns on endosomes, the punctuated structures of intermediate filaments in neurons, and nuclear protein speckles in mammalian cells with conventional optics. The reported performance of diffraction-unlimited fluorescence microscopy opens up a pathway for addressing fundamental problems in the life sciences."],["dc.identifier.doi","10.1073/pnas.0604965103"],["dc.identifier.gro","3143651"],["dc.identifier.isi","000239616400005"],["dc.identifier.pmid","16864773"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1188"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Macromolecular-scale resolution in biological fluorescence microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","267"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","278"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Sander, Bjoern"],["dc.contributor.author","Golas, Monika M."],["dc.contributor.author","Makarov, Evgeny M."],["dc.contributor.author","Brahms, Hero"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2021-03-05T08:58:09Z"],["dc.date.available","2021-03-05T08:58:09Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1016/j.molcel.2006.08.021"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80026"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","1097-2765"],["dc.title","Organization of Core Spliceosomal Components U5 snRNA Loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as Revealed by Electron Cryomicroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","c59"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations of Crystallography"],["dc.bibliographiccitation.lastpage","c60"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Strasser, A."],["dc.contributor.author","Dickmanns, A."],["dc.contributor.author","Lührmann, R."],["dc.date.accessioned","2022-03-01T11:47:02Z"],["dc.date.available","2022-03-01T11:47:02Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1107/S0108767305097473"],["dc.identifier.pii","S0108767305097473"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103890"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0108-7673"],["dc.title","Structural basis for specific recognition of the UsnRNP m 3 G-cap by snurportin1"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2416"],["dc.bibliographiccitation.issue","23-24"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","2429"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Bao, Penghui"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2020-12-10T18:20:20Z"],["dc.date.available","2020-12-10T18:20:20Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1101/gad.308163.117"],["dc.identifier.eissn","1549-5477"],["dc.identifier.issn","0890-9369"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75524"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The RES complex is required for efficient transformation of the precatalytic B spliceosome into an activated B act complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","413"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","428"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Fourmann, Jean-Baptiste"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Christian, Henning"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2017-09-07T11:47:49Z"],["dc.date.available","2017-09-07T11:47:49Z"],["dc.date.issued","2013"],["dc.description.abstract","The spliceosome is a single-turnover enzyme that needs to be dismantled after catalysis to both release the mRNA and recycle small nuclear ribonucleoproteins (snRNPs) for subsequent rounds of pre-mRNA splicing. The RNP remodeling events occurring during spliceosome disassembly are poorly understood, and the composition of the released snRNPs are only roughly known. Using purified components in vitro, we generated post-catalytic spliceosomes that can be dissociated into mRNA and the intron-lariat spliceosome (ILS) by addition of the RNA helicase Prp22 plus ATP and without requiring the step 2 proteins Slu7 and Prp18. Incubation of the isolated ILS with the RNA helicase Prp43 plus Ntr1/Ntr2 and ATP generates defined spliceosomal dissociation products: the intron-lariat, U6 snRNA, a 20-25S U2 snRNP containing SF3a/b, an 18S U5 snRNP, and the \"nineteen complex\" associated with both the released U2 snRNP and intron-lariat RNA. Our system reproduces the entire ordered disassembly phase of the spliceosome with purified components, which defines the minimum set of agents required for this process. It enabled us to characterize the proteins of the ILS by mass spectrometry and identify the ATPase action of Prp43 as necessary and sufficient for dissociation of the ILS without the involvement of Brr2 ATPase."],["dc.identifier.doi","10.1101/gad.207779.112"],["dc.identifier.gro","3142392"],["dc.identifier.isi","000315286300007"],["dc.identifier.pmid","23431055"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7774"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 860]; GGNB (DFG) [GSC 226/1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0890-9369"],["dc.title","Dissection of the factor requirements for spliceosome disassembly and the elucidation of its dissociation products using a purified splicing system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2162"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","2174"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Xiang, Shengqi"],["dc.contributor.author","Gapsys, Vytautas"],["dc.contributor.author","Kim, Hai-Young"],["dc.contributor.author","Bessonov, Sergey"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Moehlmann, Sina"],["dc.contributor.author","Klaukien, Volker"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:46:59Z"],["dc.date.available","2017-09-07T11:46:59Z"],["dc.date.issued","2013"],["dc.description.abstract","Serine/arginine-rich (SR) proteins are important players in RNA metabolism and are extensively phosphorylated at serine residues in RS repeats. Here, we show that phosphorylation switches the RS domain of the serine/arginine-rich splicing factor 1 from a fully disordered state to a partially rigidified arch-like structure. Nuclear magnetic resonance spectroscopy in combination with molecular dynamics simulations revealed that the conformational switch is restricted to RS repeats, critically depends on the phosphate charge state and strongly decreases the conformational entropy of RS domains. The dynamic switch also occurs in the 100 kDa SR-related protein hPrp28, for which phosphorylation at the RS repeat is required for spliceosome assembly. Thus, a phosphorylation-induced dynamic switch is common to the class of serine/arginine-rich proteins and provides a molecular basis for the functional redundancy of serine/arginine-rich proteins and the profound influence of RS domain phosphorylation on protein-protein and protein-RNA interactions."],["dc.identifier.doi","10.1016/j.str.2013.09.014"],["dc.identifier.gro","3142236"],["dc.identifier.isi","000328914900010"],["dc.identifier.pmid","24183573"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6043"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1878-4186"],["dc.relation.issn","0969-2126"],["dc.title","Phosphorylation Drives a Dynamic Switch in Serine/Arginine-Rich Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["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","531"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","541"],["dc.bibliographiccitation.volume","385"],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2018-11-07T08:33:29Z"],["dc.date.available","2018-11-07T08:33:29Z"],["dc.date.issued","2009"],["dc.description.abstract","The precursor mRNA retention and splicing (RES) complex mediates nuclear retention and enhances splicing of precursor mRNAs. The RES complex from yeast comprises three proteins, Snu17p, Bud13p and Pml1p. Snu17p acts as a central platform that concomitantly binds the Bud13p and Pml1p subunits via short peptide epitopes. As a step to decipher the molecular architecture of the RES complex, we have determined crystal structures of full-length Pml1p and N-terminally truncated Pml1p. The first 50 residues of full-length Pml1p, encompassing the Snu17p-binding region, are disordered, showing that Pml1p binds to Snu17p via an intrinsically unstructured region. The remainder of Pml1p folds as a forkhead-associated (FHA) domain, which is expanded by a number of noncanonical elements compared with known FHA domains from other proteins. An atypical N-terminal appendix runs across one beta-sheet and thereby stabilizes the domain as shown by deletion experiments. FHA domains are thought to constitute phosphopeptide-binding elements. Consistently, a sulfate ion was found at the putative phosphopeptide-binding loops of full-length Pml1p. The N-terminally truncated version of the protein lacked a similar phosphopeptide mimic but retained an almost identical structure. A long loop neighboring the putative phosphopeptide-binding site was disordered in both structures. Comparison with other FHA domain proteins suggests that this loop adopts a defined conformation upon ligand binding and thereby confers ligand specificity. Our results show that in the RES complex, an FHA domain of Pml1p is flexibly tethered via an unstructured N-terminal region to Snu17p. (C) 2008 Elsevier Ltd. All rights reserved."],["dc.description.sponsorship","Max Planck Society"],["dc.identifier.doi","10.1016/j.jmb.2008.10.087"],["dc.identifier.isi","000262916900016"],["dc.identifier.pmid","19010333"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17588"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","Crystal Structure of the Pml1p Subunit of the Yeast Precursor mRNA Retention and Splicing Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]