Odenwälder, Peter

[["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","47a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Orth, Thomas"],["dc.contributor.author","Odenwälder, Peter"],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.date.accessioned","2021-03-05T08:57:53Z"],["dc.date.available","2021-03-05T08:57:53Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1016/j.bpj.2011.11.287"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79918"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","0006-3495"],["dc.title","Single-Molecule Fluorescence Spectroscopy of the Structure and Dynamics of the Spliceosomal Complex"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","902"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","915"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Ohrt, Thomas"],["dc.contributor.author","Odenwälder, Peter"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Warkocki, Zbigniew"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Karaduman, Ramazan"],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-04-23T11:49:29Z"],["dc.date.available","2018-04-23T11:49:29Z"],["dc.date.issued","2013"],["dc.description.abstract","Step 2 catalysis of pre-mRNA splicing entails the excision of the intron and ligation of the 5′ and 3′ exons. The tasks of the splicing factors Prp16, Slu7, Prp18, and Prp22 in the formation of the step 2 active site of the spliceosome and in exon ligation, and the timing of their recruitment, remain poorly understood. Using a purified yeast in vitro splicing system, we show that only the DEAH-box ATPase Prp16 is required for formation of a functional step 2 active site and for exon ligation. Efficient docking of the 3′ splice site (3′SS) to the active site requires only Slu7/Prp18 but not Prp22. Spliceosome remodeling by Prp16 appears to be subtle as only the step 1 factor Cwc25 is dissociated prior to step 2 catalysis, with its release dependent on docking of the 3′SS to the active site and Prp16 action. We show by fluorescence cross-correlation spectroscopy that Slu7/Prp18 and Prp16 bind early to distinct, low-affinity binding sites on the step-1-activated B spliceosome, which are subsequently converted into high-affinity sites. Our results shed new light on the factor requirements for step 2 catalysis and the dynamics of step 1 and 2 factors during the catalytic steps of splicing."],["dc.identifier.doi","10.1261/rna.039024.113"],["dc.identifier.gro","3142126"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13707"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.doi","10.1261/rna.039024.113"],["dc.relation.issn","1355-8382"],["dc.title","Molecular dissection of step 2 catalysis of yeast pre-mRNA splicing investigated in a purified system"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1244"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1256"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Ohrt, Thomas"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Odenwälder, Peter"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Rasche, Nicolas"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-04-23T11:49:30Z"],["dc.date.available","2018-04-23T11:49:30Z"],["dc.date.issued","2012"],["dc.description.abstract","The compositional and conformational changes during catalytic activation of the spliceosome promoted by the DEAH box ATPase Prp2 are only poorly understood. Here, we show by dual-color fluorescence cross-correlation spectroscopy (dcFCCS) that the binding affinity of several proteins is significantly changed during the Prp2-mediated transition of precatalytic Bact spliceosomes to catalytically activated B spliceosomes from Saccharomyces cerevisiae. During this step, several proteins, including the zinc-finger protein Cwc24, are quantitatively displaced from the B complex. Consistent with this, we show that Cwc24 is required for step 1 but not for catalysis per se. The U2-associated SF3a and SF3b proteins Prp11 and Cus1 remain bound to the B spliceosome under near-physiological conditions, but their binding is reduced at high salt. Conversely, high-affinity binding sites are created for Yju2 and Cwc25 during catalytic activation, consistent with their requirement for step 1 catalysis. Our results suggest high cooperativity of multiple Prp2-mediated structural rearrangements at the spliceosome's catalytic core. Moreover, dcFCCS represents a powerful tool ideally suited to study quantitatively spliceosomal protein dynamics in equilibrium."],["dc.identifier.doi","10.1261/rna.033316.112"],["dc.identifier.gro","3142132"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13714"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.doi","10.1261/rna.033316.112"],["dc.relation.issn","1355-8382"],["dc.relation.issn","1355-8382"],["dc.title","Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]