{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jungwirth S"],"funding":["Deutsche Forschungsgemeinschaft (German Research Foundation)","Volkswagen Foundation (VolkswagenStiftung)"],"pagination":["1648"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12917281"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(1)"],"pubmed_abstract":["The recruitment of RNA polymerase to gene promoters is a critical step in gene expression. For RNA polymerase II, this process is initiated by TBP and TFIIB, with homologs of these TBP/TFIIB pairs found in all known multi-subunit RNA polymerase systems. Here, we describe a mode of promoter recognition by the poxviral intermediate transcription factor 3, VITF-3. This heterodimeric factor comprises an atypical TBP/TFIIB pair forming a stable ring structure inert towards DNA in the absence of viral RNA polymerase. Promoter recognition instead requires concerted VITF-3 and viral RNA polymerase binding, as shown by cryo-EM analysis of the intermediate pre-initiation complex. During the formation of this complex, viral RNA polymerase facilitates ring opening and loading of VITF-3 onto the promot"],"journal":["Nature communications"],"pubmed_title":["Cooperative clamp-mediated promoter recognition by poxviral RNA polymerase and its TBP/TFIIB-like partner."],"pmcid":["PMC12917281"],"funding_grant_id":["9B813","Fi 573/27-1"],"pubmed_authors":["Fischer U","Schlosser A","Lamer S","Bartuli J","Grimm C","Jungwirth S"],"additional_accession":[]},"is_claimable":false,"name":"Cooperative clamp-mediated promoter recognition by poxviral RNA polymerase and its TBP/TFIIB-like partner.","description":"The recruitment of RNA polymerase to gene promoters is a critical step in gene expression. For RNA polymerase II, this process is initiated by TBP and TFIIB, with homologs of these TBP/TFIIB pairs found in all known multi-subunit RNA polymerase systems. Here, we describe a mode of promoter recognition by the poxviral intermediate transcription factor 3, VITF-3. This heterodimeric factor comprises an atypical TBP/TFIIB pair forming a stable ring structure inert towards DNA in the absence of viral RNA polymerase. Promoter recognition instead requires concerted VITF-3 and viral RNA polymerase binding, as shown by cryo-EM analysis of the intermediate pre-initiation complex. During the formation of this complex, viral RNA polymerase facilitates ring opening and loading of VITF-3 onto the promot","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T10:06:11.679Z","creation":"2026-07-09T10:48:55.034Z"},"accession":"S-EPMC12917281","cross_references":{"pubmed":["41708602"],"doi":["10.1038/s41467-026-69571-1"]}}