Evidence map›Paper›PMID 33243850›Full record

ArticleScience (New York, N.Y.)2021

Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ.

Nelly Said, Tarek Hilal, Nicholas D Sunday, Ajay Khatri, Jörg Bürger, Thorsten Mielke, Georgiy A Belogurov, Bernhard Loll, Ranjan Sen, Irina Artsimovitch and 1 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
–field-weighted citation impact
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

78 citing papers in PubMed.

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18 more citing papers are in PubMed but not listed here.

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

11 authors.

Nelly Said *Laboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.ORCID https://orcid.org/0000-0001-8352-5555
Tarek Hilal *Research Center of Electron Microscopy and Core Facility BioSupraMol, Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.ORCID https://orcid.org/0000-0002-7833-8058
Nicholas D SundayDepartment of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, OH, USA.ORCID https://orcid.org/0000-0003-1012-160X
Ajay KhatriLaboratory of Transcription, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, India.
Jörg BürgerMicroscopy and Cryo-Electron Microscopy Service Group, Max-Planck-Institut für Molekulare Genetik, Berlin, Germany.
Thorsten MielkeMicroscopy and Cryo-Electron Microscopy Service Group, Max-Planck-Institut für Molekulare Genetik, Berlin, Germany.ORCID https://orcid.org/0000-0001-9275-3146
Georgiy A BelogurovDepartment of Biochemistry, University of Turku, FIN-20014 Turku, Finland.ORCID https://orcid.org/0000-0002-3070-6843
Bernhard LollLaboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.ORCID https://orcid.org/0000-0001-7928-4488
Ranjan SenLaboratory of Transcription, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, India.ORCID https://orcid.org/0000-0001-5693-787X
Irina ArtsimovitchDepartment of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, OH, USA. artsimovitch.1@osu.edu markus.wahl@fu-berlin.de.ORCID https://orcid.org/0000-0002-8604-0980
Markus C WahlLaboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany. artsimovitch.1@osu.edu markus.wahl@fu-berlin.de.ORCID https://orcid.org/0000-0002-2811-5307

Funding

Mechnanism of transcript elongation control by RfaHR01GM067153 · NIGMS · OHIO STATE UNIVERSITY · PI IRINA ARTSIMOVITCH · 2003 to 2026
$8.0M
NIGMS NIH HHS R01 GM067153
6 · The paper itself

Abstract

Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ρ on a pathway to terminating NusA/NusG-modified elongation complexes. An open ρ ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the ρ ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping ρ subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that ρ, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state.

Indexed as

Transcription Elongation, GeneticAdenosine TriphosphatasesCryoelectron MicroscopyDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsMultiprotein ComplexesPeptide Elongation FactorsProtein ConformationProtein TransportRho FactorTranscriptional Elongation FactorsTranscription FactorsZinc FingersAdenosine TriphosphatasesDNA-Directed RNA PolymerasesEscherichia coli ProteinsMultiprotein ComplexesnusA protein, E coliNusG protein, E coliPeptide Elongation FactorsRho FactorTranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID33243850
PMCPMC7864586

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.