Schilbach, Sandra

[["dc.bibliographiccitation.firstpage","103754"],["dc.bibliographiccitation.journal","Journal of Proteomics"],["dc.bibliographiccitation.volume","220"],["dc.contributor.author","Parfentev, Iwan"],["dc.contributor.author","Schilbach, Sandra"],["dc.contributor.author","Cramer, Patrick"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2020-12-10T14:25:18Z"],["dc.date.available","2020-12-10T14:25:18Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1016/j.jprot.2020.103754"],["dc.identifier.pmid","32201362"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72524"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/111"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/74"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A06: Mitochondrienfunktion und -umsatz in Synapsen"],["dc.relation.workinggroup","RG Cramer"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.title","An experimentally generated peptide database increases the sensitivity of XL-MS with complex samples"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.contributor.author","Rengachari, Srinivasan"],["dc.contributor.author","Schilbach, Sandra"],["dc.contributor.author","Kaliyappan, Thangavelu"],["dc.contributor.author","Gouge, Jerome"],["dc.contributor.author","Zumer, Kristina"],["dc.contributor.author","Schwarz, Juliane"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Dienemann, Christian"],["dc.contributor.author","Vannini, Alessandro"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2022-12-01T08:30:54Z"],["dc.date.available","2022-12-01T08:30:54Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n RNA polymerase II (Pol II) carries out transcription of both protein-coding and non-coding genes. Whereas Pol II initiation at protein-coding genes has been studied in detail, Pol II initiation at non-coding genes, such as small nuclear RNA (snRNA) genes, is less well understood at the structural level. Here, we study Pol II initiation at snRNA gene promoters and show that the snRNA-activating protein complex (SNAPc) enables DNA opening and transcription initiation independent of TFIIE and TFIIH in vitro. We then resolve cryo-EM structures of the SNAPc-containing Pol IIpre-initiation complex (PIC) assembled on U1 and U5 snRNA promoters. The core of SNAPc binds two turns of DNA and recognizes the snRNA promoter-specific proximal sequence element (PSE), located upstream of the TATA box-binding protein TBP. Two extensions of SNAPc, called wing-1 and wing-2, bind TFIIA and TFIIB, respectively, explaining how SNAPc directs Pol II to snRNA promoters. Comparison of structures of closed and open promoter complexes elucidates TFIIH-independent DNA opening. These results provide the structural basis of Pol II initiation at non-coding RNA gene promoters."],["dc.identifier.doi","10.1038/s41594-022-00857-w"],["dc.identifier.pii","857"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118010"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Structural basis of SNAPc-dependent snRNA transcription initiation by RNA polymerase II"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","97"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","106.e4"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Dienemann, Christian"],["dc.contributor.author","Schwalb, Björn"],["dc.contributor.author","Schilbach, Sandra"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2022-03-01T11:45:17Z"],["dc.date.available","2022-03-01T11:45:17Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.molcel.2018.10.014"],["dc.identifier.pii","S1097276518308463"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103276"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","1097-2765"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Promoter Distortion and Opening in the RNA Polymerase II Cleft"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.contributor.author","Wang, Haibo"],["dc.contributor.author","Schilbach, Sandra"],["dc.contributor.author","Ninov, Momchil"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2022-12-01T08:30:54Z"],["dc.date.available","2022-12-01T08:30:54Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n \n The preinitiation complex (PIC) assembles on promoters of protein-coding genes to position RNA polymerase II (Pol II) for transcription initiation. Previous structural studies revealed the PIC on different promoters, but did not address how the PIC assembles within chromatin. In the yeast\n Saccharomyces cerevisiae\n , PIC assembly occurs adjacent to the +1 nucleosome that is located downstream of the core promoter. Here we present cryo-EM structures of the yeast PIC bound to promoter DNA and the +1 nucleosome located at three different positions. The general transcription factor TFIIH engages with the incoming downstream nucleosome and its translocase subunit Ssl2 (XPB in human TFIIH) drives the rotation of the +1 nucleosome leading to partial detachment of nucleosomal DNA and intimate interactions between TFIIH and the nucleosome. The structures provide insights into how transcription initiation can be influenced by the +1 nucleosome and may explain why the transcription start site is often located roughly 60 base pairs upstream of the dyad of the +1 nucleosome in yeast."],["dc.identifier.doi","10.1038/s41594-022-00865-w"],["dc.identifier.pii","865"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118011"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Structures of transcription preinitiation complex engaged with the +1 nucleosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","204"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","209"],["dc.bibliographiccitation.volume","551"],["dc.contributor.author","Schilbach, S."],["dc.contributor.author","Hantsche, M."],["dc.contributor.author","Tegunov, D."],["dc.contributor.author","Dienemann, C."],["dc.contributor.author","Wigge, C."],["dc.contributor.author","Urlaub, H."],["dc.contributor.author","Cramer, P."],["dc.date.accessioned","2018-01-09T12:04:30Z"],["dc.date.available","2018-01-09T12:04:30Z"],["dc.date.issued","2017"],["dc.description.abstract","For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC-core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the 'E-bridge' helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC-core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II."],["dc.identifier.doi","10.1038/nature24282"],["dc.identifier.pmid","29088706"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11583"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1476-4687"],["dc.title","Structures of transcription pre-initiation complex with TFIIH and Mediator"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]