Evidence map›Paper›PMID 24598909›Full record

ArticleNature communications2014

CBR antimicrobials alter coupling between the bridge helix and the β subunit in RNA polymerase.

Anssi M Malinen, Monali Nandymazumdar, Matti Turtola, Henri Malmi, Thadee Grocholski, Irina Artsimovitch, Georgiy A Belogurov

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-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

32 citing papers in PubMed, 42 citations in OpenAlex.

  1. RNA polymerase inhibitors reveal active-site motions essential for the nucleotide addition cycle.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
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  4. Review
  5. Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025
    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

7 authors at 2 institutions in 2 countries.

Anssi M MalinenDepartment of Biochemistry, University of Turku, Turku 20014, Finland.
Monali NandymazumdarDepartment of Microbiology, The Ohio State University, Columbus, Ohio 43210, USA.
Matti TurtolaDepartment of Biochemistry, University of Turku, Turku 20014, Finland.
Henri MalmiDepartment of Biochemistry, University of Turku, Turku 20014, Finland.
Thadee GrocholskiDepartment of Biochemistry, University of Turku, Turku 20014, Finland.
Irina ArtsimovitchDepartment of Microbiology, The Ohio State University, Columbus, Ohio 43210, USA.
Georgiy A BelogurovDepartment of Biochemistry, University of Turku, Turku 20014, Finland.
University of Turku · FIThe Ohio State University · US

Funding

Mechnanism of transcript elongation control by RfaHR01GM067153 · NIGMS · OHIO STATE UNIVERSITY · PI IRINA ARTSIMOVITCH · 2003 to 2026
$8.0M
NIGMS NIH HHS GM067153NIGMS NIH HHS R01 GM067153
6 · The paper itself

Abstract

Bacterial RNA polymerase (RNAP) is a validated target for antibacterial drugs. CBR703 series antimicrobials allosterically inhibit transcription by binding to a conserved α helix (β' bridge helix, BH) that interconnects the two largest RNAP subunits. Here we show that disruption of the BH-β subunit contacts by amino-acid substitutions invariably results in accelerated catalysis, slowed-down forward translocation and insensitivity to regulatory pauses. CBR703 partially reverses these effects in CBR-resistant RNAPs while inhibiting catalysis and promoting pausing in CBR-sensitive RNAPs. The differential response of variant RNAPs to CBR703 suggests that the inhibitor binds in a cavity walled by the BH, the β' F-loop and the β fork loop. Collectively, our data are consistent with a model in which the β subunit fine tunes RNAP elongation activities by altering the BH conformation, whereas CBRs deregulate transcription by increasing coupling between the BH and the β subunit.

Indexed as

AmidinesAmino Acid SubstitutionAnti-Infective AgentsBacterial ProteinsBiocatalysisDNA-Directed RNA PolymerasesHydroxylaminesKineticsModels, MolecularMolecular StructureProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsAmidinesAnti-Infective AgentsBacterial ProteinsCBR 703DNA-Directed RNA PolymerasesHydroxylaminesProtein Subunits

Identifiers

PMID24598909
PMCPMC3959191
OpenAlexW2049917954

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.