Evidence map›Paper›PMID 34556871›Full record

ArticleNature structural & molecular biology2021

Structural basis of the complete poxvirus transcription initiation process.

Clemens Grimm, Julia Bartuli, Bettina Boettcher, Aladar A Szalay, Utz Fischer

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Host transfer RNA guides assembly of viral RNA polymerase.Nature structural & molecular biology · 2025
    Article
  4. Article
  5. Article
  6. Methods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
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  13. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Clemens Grimm *Department of Biochemistry and Cancer Therapy Research Center (CTRC), Theodor Boveri-Institute, University of Würzburg, Würzburg, Germany. clemens.grimm@biozentrum.uni-wuerzburg.de.ORCID http://orcid.org/0000-0001-9085-5130
Julia Bartuli *Department of Biochemistry and Cancer Therapy Research Center (CTRC), Theodor Boveri-Institute, University of Würzburg, Würzburg, Germany.
Bettina BoettcherDepartment of Biochemistry, Rudolf-Virchow-Center, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0002-7962-4849
Aladar A SzalayDepartment of Biochemistry and Cancer Therapy Research Center (CTRC), Theodor Boveri-Institute, University of Würzburg, Würzburg, Germany.
Utz FischerDepartment of Biochemistry and Cancer Therapy Research Center (CTRC), Theodor Boveri-Institute, University of Würzburg, Würzburg, Germany. utz.fischer@biozentrum.uni-wuerzburg.de.ORCID http://orcid.org/0000-0002-1465-6591
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poxviruses 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.

Indexed as

Transcription Initiation, GeneticAdenosine TriphosphateCryoelectron MicroscopyDNA-Directed RNA PolymerasesDNA HelicasesDNA, ViralGene Expression Regulation, ViralHeLa CellsHumansModels, MolecularPromoter Regions, GeneticProtein DomainsProtein SubunitsTranscription FactorsVaccinia virusViral ProteinsAdenosine TriphosphateDNA-Directed RNA PolymerasesDNA HelicasesDNA, ViralProtein SubunitsTranscription FactorsViral Proteins

Identifiers

PMID34556871
OpenAlexW3158044476

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.