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dc.contributor.authorKramm, K
dc.contributor.authorSchröder, T
dc.contributor.authorGouge, J
dc.contributor.authorVera, AM
dc.contributor.authorGupta, K
dc.contributor.authorHeiss, FB
dc.contributor.authorLiedl, T
dc.contributor.authorEngel, C
dc.contributor.authorBerger, I
dc.contributor.authorVannini, A
dc.contributor.authorTinnefeld, P
dc.contributor.authorGrohmann, D
dc.date.accessioned2020-07-06T14:34:25Z
dc.date.issued2020-06-05
dc.identifier.citationNature communications, 2020, 11 (1), pp. 2828 - ?
dc.identifier.issn2041-1723
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3814
dc.identifier.eissn2041-1723
dc.identifier.doi10.1038/s41467-020-16702-x
dc.description.abstractThe TATA-binding protein (TBP) and a transcription factor (TF) IIB-like factor are important constituents of all eukaryotic initiation complexes. The reason for the emergence and strict requirement of the additional initiation factor Bdp1 in the RNA polymerase (RNAP) III system, however, remained elusive. A poorly studied aspect in this context is the effect of DNA strain arising from DNA compaction and transcriptional activity on initiation complex formation. We made use of a DNA origami-based force clamp to follow the assembly of human initiation complexes in the RNAP II and RNAP III systems at the single-molecule level under piconewton forces. We demonstrate that TBP-DNA complexes are force-sensitive and TFIIB is sufficient to stabilise TBP on a strained promoter. In contrast, Bdp1 is the pivotal component that ensures stable anchoring of initiation factors, and thus the polymerase itself, in the RNAP III system. Thereby, we offer an explanation for the crucial role of Bdp1 for the high transcriptional output of RNAP III.
dc.formatElectronic
dc.format.extent2828 - ?
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectRNA Polymerase III
dc.subjectTATA-Box Binding Protein
dc.subjectTranscription Factor TFIIIB
dc.subjectRecombinant Proteins
dc.subjectDNA, Single-Stranded
dc.subjectMolecular Probes
dc.subjectMicroscopy, Confocal
dc.subjectMicroscopy, Electron, Transmission
dc.subjectFluorescence Resonance Energy Transfer
dc.subjectTranscription, Genetic
dc.subjectNucleic Acid Conformation
dc.subjectKinetics
dc.subjectPromoter Regions, Genetic
dc.subjectProtein Stability
dc.subjectSingle Molecule Imaging
dc.titleDNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability.
dc.typeJournal Article
dcterms.dateAccepted2020-05-13
rioxxterms.versionofrecord10.1038/s41467-020-16702-x
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2020-06-05
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfNature communications
pubs.issue1
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Vannini Group
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Vannini Group
pubs.publication-statusPublished
pubs.volume11en_US
pubs.embargo.termsNot known
icr.researchteamVannini Groupen_US
dc.contributor.icrauthorVannini, Alessandroen


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