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Cooperative clamp-mediated promoter recognition by poxviral RNA polymerase and its TBP/TFIIB-like partner

ABSTRACT: The recruitment of RNA polymerase (RNAP) to gene promoters is a critical step in gene expression. For RNAP II, this process is initiated by the TATA-box binding protein (TBP) and transcription factor IIB (TFIIB), with homologs of these TBP/TFIIB pairs found in all known multi-subunit RNAP systems. Here we describe a previously unknown 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 RNAP (vRNAP). Promoter recognition instead requires concerted VITF-3 and vRNAP binding, as revealed by cryo-EM analysis of the intermediate pre-initiation complex (iPIC). During iPIC formation, vRNAP facilitates ring opening and loading of VITF-3 onto the promoter, anchoring the polymerase at the transcription start site. Our findings propose vRNAP as a clamp loader for VITF-3 and reveal a thus far unknown transcription initiation mechanism.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human) Vaccinia Virus

SUBMITTER: Stefan Jungwirth

LAB HEAD: Utz Fischer

PROVIDER: PXD065561 | Pride | 2025-12-17

REPOSITORIES: Pride

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			Action	DRS
	2022-12-21_Fusion_35608.raw	Raw
	2022-12-21_Fusion_35613.raw	Raw
	2025-03-21_Fusion_46471.raw	Raw
	2025-03-21_Fusion_46475.raw	Raw
	2025-03-21_Fusion_46481.raw	Raw

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