Show simple item record

dc.contributor.authorGrimm, Clemens
dc.contributor.authorBartuli, Julia
dc.contributor.authorBoettcher, Bettina
dc.contributor.authorSzalay, Aladar A
dc.contributor.authorFischer, Utz
dc.date.accessioned2021-11-10T15:11:32Z
dc.date.available2021-11-10T15:11:32Z
dc.date.issued2021-09-23
dc.identifier.citationNat Struct Mol Biol. 2021 Oct;28(10):779-788. doi: 10.1038/s41594-021-00655-w. Epub 2021 Sep 23.en_US
dc.identifier.pmid34556871
dc.identifier.doi10.1038/s41594-021-00655-w
dc.identifier.urihttp://hdl.handle.net/10033/623091
dc.description.abstractPoxviruses express their genes in the cytoplasm of infected cells using a virus-encoded multi-subunit polymerase (vRNAP) and unique transcription factors. We present cryo-EM structures that uncover the complete transcription initiation phase of the poxvirus vaccinia. In the pre-initiation complex, the heterodimeric early transcription factor VETFs/l adopts an arc-like shape spanning the polymerase cleft and anchoring upstream and downstream promoter elements. VETFI emerges as a TBP-like protein that inserts asymmetrically into the DNA major groove, triggers DNA melting, ensures promoter recognition and enforces transcription directionality. The helicase VETFs fosters promoter melting and the phospho-peptide domain (PPD) of vRNAP subunit Rpo30 enables transcription initiation. An unprecedented upstream promoter scrunching mechanism assisted by the helicase NPH-I probably fosters promoter escape and transition into elongation. Our structures shed light on unique mechanisms of poxviral gene expression and aid the understanding of thus far unexplained universal principles in transcription.en_US
dc.language.isoenen_US
dc.publisherNature reseachen_US
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.titleStructural basis of the complete poxvirus transcription initiation process.en_US
dc.typeArticleen_US
dc.identifier.eissn1545-9985
dc.contributor.departmentCiiM, Zentrum für individualisierte Infektionsmedizin, Feodor-Lynen-Str.7, 30625 Hannover.en_US
dc.identifier.journalNature structural & molecular biologyen_US
dc.source.volume28
dc.source.issue10
dc.source.beginpage779
dc.source.endpage788
refterms.dateFOA2021-11-10T15:11:33Z
dc.source.journaltitleNature structural & molecular biology
dc.source.countryUnited States


Files in this item

Thumbnail
Name:
Grimm et al.pdf
Size:
6.954Mb
Format:
PDF
Description:
Open Access publication

This item appears in the following Collection(s)

Show simple item record

Attribution 4.0 International
Except where otherwise noted, this item's license is described as Attribution 4.0 International