Evidence map›Paper›PMID 33339820›Full record

ArticleNature communications2020

Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.

Timothy P Newing, Aaron J Oakley, Michael Miller, Catherine J Dawson, Simon H J Brown, James C Bouwer, Gökhan Tolun, Peter J Lewis

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

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  3. Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

8 authors at 2 institutions in 1 country.

Timothy P NewingMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia.ORCID 0000-0002-7147-6984
Aaron J OakleyMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia.ORCID 0000-0002-4764-014X
Michael MillerSchool of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, 2308, Australia.ORCID 0000-0001-7990-3381
Catherine J DawsonSchool of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, 2308, Australia.ORCID 0000-0002-9780-4130
Simon H J BrownMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia.ORCID 0000-0003-3997-4614
James C BouwerMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia.ORCID 0000-0003-2384-070X
Gökhan TolunMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research Institute, Wollongong, NSW, 2522, Australia. gokhan_tolun@uow.edu.au.ORCID 0000-0001-6166-9451
Peter J LewisSchool of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, 2308, Australia. Peter.Lewis@newcastle.edu.au.ORCID 0000-0002-1992-062X
University of Wollongong · AUUniversity of Newcastle Australia · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In bacteria, transcription complexes stalled on DNA represent a major source of roadblocks for the DNA replication machinery that must be removed in order to prevent damaging collisions. Gram-positive bacteria contain a transcription factor HelD that is able to remove and recycle stalled complexes, but it was not known how it performed this function. Here, using single particle cryo-electron microscopy, we have determined the structures of Bacillus subtilis RNA polymerase (RNAP) elongation and HelD complexes, enabling analysis of the conformational changes that occur in RNAP driven by HelD interaction. HelD has a 2-armed structure which penetrates deep into the primary and secondary channels of RNA polymerase. One arm removes nucleic acids from the active site, and the other induces a large conformational change in the primary channel leading to removal and recycling of the stalled polymerase, representing a novel mechanism for recycling transcription complexes in bacteria.

Indexed as

Transcription, GeneticBacillus subtilisBacterial ProteinsCryoelectron MicroscopyDNA-Directed RNA PolymerasesImaging, Three-DimensionalModels, MolecularProtein BindingTranscription Elongation, GeneticBacterial ProteinsDNA-Directed RNA Polymerases

Identifiers

PMID33339820
PMCPMC7749167
OpenAlexW3114941018

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.