Evidence map›Paper›PMID 19356588›Full record

ArticleJournal of molecular biology2009

Coupling sigma factor conformation to RNA polymerase reorganisation for DNA melting.

Patricia C Burrows, Nicolas Joly, Wendy V Cannon, Beatriz P Cámara, Mathieu Rappas, Xiaodong Zhang, Kathleen Dawes, B Tracy Nixon, Siva R Wigneshweraraj, Martin Buck

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Real-time capture of σNature communications · 2025
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  5. Review
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  7. A prehydrolysis state of an AAA+ ATPase supports transcription activation of an enhancer-dependent RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2010
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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

10 authors at 2 institutions in 2 countries.

Patricia C BurrowsDivision of Biology, Department of Life Sciences, Faculty of Natural Sciences, Sir Alexander Fleming Building, Imperial College London, London SW7 2AZ, UK.
Nicolas Joly
Wendy V Cannon
Beatriz P Cámara
Mathieu Rappas
Xiaodong Zhang
Kathleen Dawes
B Tracy Nixon
Siva R Wigneshweraraj
Martin Buck
Imperial College London · GBPennsylvania State University · US

Funding

Elucidating the Conformational Dynamics of the AAA+ ATPases NtrC1 and NtrCR01GM069937 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI NIXON, B TRACY · 2006 to 2009
$1.3M
Biotechnology and Biological Sciences Research Council BB/D521922/1Biotechnology and Biological Sciences Research Council BB/E023703/1NIGMS NIH HHS GM069937NIGMS NIH HHS R01 GM069937Wellcome Trust
6 · The paper itself

Abstract

ATP-driven remodelling of initial RNA polymerase (RNAP) promoter complexes occurs as a major post recruitment strategy used to control gene expression. Using a model-enhancer-dependent bacterial system (sigma54-RNAP, Esigma54) and a slowly hydrolysed ATP analogue (ATPgammaS), we provide evidence for a nucleotide-dependent temporal pathway leading to DNA melting involving a small set of sigma54-DNA conformational states. We demonstrate that the ATP hydrolysis-dependent remodelling of Esigma54 occurs in at least two distinct temporal steps. The first detected remodelling phase results in changes in the interactions between the promoter specificity sigma54 factor and the promoter DNA. The second detected remodelling phase causes changes in the relationship between the promoter DNA and the core RNAP catalytic beta/beta' subunits, correlating with the loading of template DNA into the catalytic cleft of RNAP. It would appear that, for Esigma54 promoters, loading of template DNA within the catalytic cleft of RNAP is dependent on fast ATP hydrolysis steps that trigger changes in the beta' jaw domain, thereby allowing acquisition of the open complex status.

Indexed as

Nucleic Acid DenaturationAdenosine TriphosphatasesAdenosine TriphosphateBase SequenceDNA, BacterialEscherichia coliEscherichia coli ProteinsHydrolysisKlebsiella pneumoniaeMolecular Sequence DataMutant ProteinsNucleic Acid ConformationProtein ConformationProtein Structure, TertiaryProtein SubunitsRNA Polymerase Sigma 54adenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphatasesAdenosine TriphosphateDNA, BacterialEscherichia coli ProteinsMutant ProteinsProtein SubunitsPspF protein, E coliRNA Polymerase Sigma 54Trans-Activators

Identifiers

PMID19356588
PMCPMC2688459
OpenAlexW1988707178

What OpenQuestion holds

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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.