Ficner, Ralf

[["dc.bibliographiccitation.artnumber","102144"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.contributor.author","Heidemann, Jana L."],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Krüger, Larissa"],["dc.contributor.author","Wicke, Dennis"],["dc.contributor.author","Vinhoven, Liza"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-07-01T07:35:47Z"],["dc.date.available","2022-07-01T07:35:47Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.jbc.2022.102144"],["dc.identifier.pii","S0021925822005865"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112267"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.issn","0021-9258"],["dc.title","Structural basis for c-di-AMP-dependent regulation of the bacterial stringent response by receptor protein DarB"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.contributor.author","Sievers, Katharina"],["dc.contributor.author","Welp, Luisa"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2021-09-01T06:42:13Z"],["dc.date.available","2021-09-01T06:42:13Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1080/15476286.2021.1950980"],["dc.identifier.pmid","34241577"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89006"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/320"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.title","Structural and functional insights into human tRNA guanine transgylcosylase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["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","5581"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5593"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Kuehn-Hoelsken, Eva"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Richter, Florian M."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2017-09-07T11:45:20Z"],["dc.date.available","2017-09-07T11:45:20Z"],["dc.date.issued","2010"],["dc.description.abstract","Mass spectrometry allows the elucidation of molecular details of the interaction domains of the individual components in macromolecular complexes subsequent to cross-linking of the individual components. Here, we applied chemical and UV cross-linking combined with tandem mass-spectrometric analysis to identify contact sites of the nuclear import adaptor snurportin 1 to the small ribonucleoprotein particle U1 snRNP in addition to the known interaction of m(3)G cap and snurportin 1. We were able to define previously unknown sites of protein-protein and protein-RNA interactions on the molecular level within U1 snRNP. We show that snurportin 1 interacts with its central m(3)G-cap-binding domain with Sm proteins and with its extreme C-terminus with stem-loop III of U1 snRNA. The crosslinking data support the idea of a larger interaction area between snurportin 1 and U snRNPs and the contact sites identified prove useful for modeling the spatial arrangement of snurportin 1 domains when bound to U1 snRNP. Moreover, this suggests a functional nuclear import complex that assembles around the m(3)G cap and the Sm proteins only when the Sm proteins are bound and arranged in the proper orientation to the cognate Sm site in U snRNA."],["dc.identifier.doi","10.1093/nar/gkq272"],["dc.identifier.gro","3142869"],["dc.identifier.isi","000281720500034"],["dc.identifier.pmid","20421206"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/320"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0305-1048"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Mapping the binding site of snurportin 1 on native U1 snRNP by cross-linking and mass spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1237"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U50"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Warkocki, Zbigniew"],["dc.contributor.author","Odenwaelder, Peter"],["dc.contributor.author","Schmitzova, Jana"],["dc.contributor.author","Platzmann, Florian"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.date.accessioned","2017-09-07T11:46:45Z"],["dc.date.available","2017-09-07T11:46:45Z"],["dc.date.issued","2009"],["dc.description.abstract","The spliceosome is a ribonucleoprotein machine that removes introns from pre-mRNA in a two-step reaction. To investigate the catalytic steps of splicing, we established an in vitro splicing complementation system. Spliceosomes stalled before step 1 of this process were purified to near-homogeneity from a temperature-sensitive mutant of the RNA helicase Prp2, compositionally defined, and shown to catalyze efficient step 1 when supplemented with recombinant Prp2, Spp2 and Cwc25, thereby demonstrating that Cwc25 has a previously unknown role in promoting step 1. Step 2 catalysis additionally required Prp16, Slu7, Prp18 and Prp22. Our data further suggest that Prp2 facilitates catalytic activation by remodeling the spliceosome, including destabilizing the SF3a and SF3b proteins, likely exposing the branch site before step 1. Remodeling by Prp2 was confirmed by negative stain EM and image processing. This system allows future mechanistic analyses of spliceosome activation and catalysis."],["dc.identifier.doi","10.1038/nsmb.1729"],["dc.identifier.gro","3143021"],["dc.identifier.isi","000272609200010"],["dc.identifier.pmid","19935684"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/489"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9993"],["dc.title","Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","690"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","702"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Port, Sarah A."],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Spillner, Christiane"],["dc.contributor.author","Hofele, Romina"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.date.accessioned","2017-09-07T11:43:28Z"],["dc.date.available","2017-09-07T11:43:28Z"],["dc.date.issued","2015"],["dc.description.abstract","CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tightly interacts with the nucleoporin Nup214. Here, we present the crystal structure of a 117-amino-acid FG-repeat-containing fragment of Nup214, in complex with CRM1, Snurportin 1, and RanGTP at 2.85 angstrom resolution. The structure reveals eight binding sites for Nup214 FG motifs on CRM1, with intervening stretches that are loosely attached to the transport receptor. Nup214 binds to N- and C-terminal regions of CRM1, thereby clamping CRM1 in a closed conformation and stabilizing the export complex. The role of conserved hydrophobic pockets for the recognition of FG motifs was analyzed in biochemical and cell-based assays. Comparative studies with RanBP3 and Nup62 shed light on specificities of CRM1-nucleoporin binding, which serves as a paradigm for transport receptor-nucleoporin interactions."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1016/j.celrep.2015.09.042"],["dc.identifier.gro","3141804"],["dc.identifier.isi","000363780900006"],["dc.identifier.pmid","26489467"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12544"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1257"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","s25"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations of Crystallography"],["dc.bibliographiccitation.lastpage","s25"],["dc.bibliographiccitation.volume","66"],["dc.contributor.author","Schulz, Eike C."],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schmitt, Andreas"],["dc.contributor.author","Mühlenhoff, Martina"],["dc.contributor.author","Stummeyer, Katharina"],["dc.contributor.author","Schwarzer, David"],["dc.contributor.author","Gerardy-Schahn, Rita"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-03-01T11:47:04Z"],["dc.date.available","2022-03-01T11:47:04Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1107/S0108767310099460"],["dc.identifier.pii","S0108767310099460"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103899"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0108-7673"],["dc.rights.uri","http://journals.iucr.org/services/copyrightpolicy.html"],["dc.title","Structure of an intramolecular chaperone mediating triple-β-helix folding"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","210"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U11"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Schulz, Eike Christian"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schmitt, Andreas"],["dc.contributor.author","Muehlenhoff, Martina"],["dc.contributor.author","Stummeyer, Katharina"],["dc.contributor.author","Schwarzer, David"],["dc.contributor.author","Gerardy-Schahn, Rita"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:46:09Z"],["dc.date.available","2017-09-07T11:46:09Z"],["dc.date.issued","2010"],["dc.description.abstract","Protein folding is often mediated by molecular chaperones. Recently, a novel class of intramolecular chaperones has been identified in tailspike proteins of evolutionarily distant viruses, which require a C-terminal chaperone for correct folding. The highly homologous chaperone domains are interchangeable between pre-proteins and release themselves after protein folding. Here we report the crystal structures of two intramolecular chaperone domains in either the released or the pre-cleaved form, revealing the role of the chaperone domain in the formation of a triple-beta-helix fold. Tentacle-like protrusions enclose the polypeptide chains of the pre-protein during the folding process. After the assembly, a sensory mechanism for correctly folded beta-helices triggers a serine-lysine catalytic dyad to autoproteolytically release the mature protein. Sequence analysis shows a conservation of the intramolecular chaperones in functionally unrelated proteins sharing beta-helices as a common structural motif."],["dc.identifier.doi","10.1038/nsmb.1746"],["dc.identifier.gro","3142975"],["dc.identifier.isi","000274228400013"],["dc.identifier.pmid","20118935"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/438"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1545-9993"],["dc.title","Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","14"],["dc.contributor.author","Blersch, Katharina F."],["dc.contributor.author","Burchert, Jan-Philipp"],["dc.contributor.author","Gleber, Sophie-Charlotte"],["dc.contributor.author","Welp, Luisa"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2021-07-05T14:57:30Z"],["dc.date.available","2021-07-05T14:57:30Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1080/15476286.2021.1925477"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87663"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-441"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.title","Structural model of the M7G46 Methyltransferase TrmB in complex with tRNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]