Evidence map›Paper›PMID 25999346›Full record

ArticleNucleic acids research2015

ATP-dependent motor activity of the transcription termination factor Rho from Mycobacterium tuberculosis.

François D'Heygère, Annie Schwartz, Franck Coste, Bertrand Castaing, Marc Boudvillain

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Multi-omics analyses of evolvedSynthetic and systems biotechnology · 2026
    Article
  3. Review
  4. Article
  5. Evolution of pH-sensitive transcription termination inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Factor-dependent archaeal transcription termination.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Article
  14. Transcription Regulation in Archaea.Journal of bacteriology · 2016
    Review
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 2 institutions in 1 country.

François D'HeygèreCentre de Biophysique Moléculaire, CNRS UPR4301, rue Charles Sadron, 45071 Orléans cedex 2, France Ecole doctorale Santé, Sciences Biologiques et Chimie du Vivant (ED 549), Université d'Orléans, Orléans, France.
Annie SchwartzCentre de Biophysique Moléculaire, CNRS UPR4301, rue Charles Sadron, 45071 Orléans cedex 2, France.
Franck CosteCentre de Biophysique Moléculaire, CNRS UPR4301, rue Charles Sadron, 45071 Orléans cedex 2, France.
Bertrand CastaingCentre de Biophysique Moléculaire, CNRS UPR4301, rue Charles Sadron, 45071 Orléans cedex 2, France ITP Sciences Biologiques & Chimie du Vivant, Université d'Orléans, Orléans, France.
Marc BoudvillainCentre de Biophysique Moléculaire, CNRS UPR4301, rue Charles Sadron, 45071 Orléans cedex 2, France ITP Sciences Biologiques & Chimie du Vivant, Université d'Orléans, Orléans, France marc.boudvillain@cnrs-orleans.fr.ORCID http://orcid.org/0000-0002-6398-9122
Université d'Orléans · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial transcription termination factor Rho-a ring-shaped molecular motor displaying directional, ATP-dependent RNA helicase/translocase activity-is an interesting therapeutic target. Recently, Rho from Mycobacterium tuberculosis (MtbRho) has been proposed to operate by a mechanism uncoupled from molecular motor action, suggesting that the manner used by Rho to dissociate transcriptional complexes is not conserved throughout the bacterial kingdom. Here, however, we demonstrate that MtbRho is a bona fide molecular motor and directional helicase which requires a catalytic site competent for ATP hydrolysis to disrupt RNA duplexes or transcription elongation complexes. Moreover, we show that idiosyncratic features of the MtbRho enzyme are conferred by a large, hydrophilic insertion in its N-terminal 'RNA binding' domain and by a non-canonical R-loop residue in its C-terminal 'motor' domain. We also show that the 'motor' domain of MtbRho has a low apparent affinity for the Rho inhibitor bicyclomycin, thereby contributing to explain why M. tuberculosis is resistant to this drug. Overall, our findings support that, in spite of adjustments of the Rho motor to specific traits of its hosting bacterium, the basic principles of Rho action are conserved across species and could thus constitute pertinent screening criteria in high-throughput searches of new Rho inhibitors.

Indexed as

Transcription Termination, GeneticAdenosine TriphosphatasesAdenosine TriphosphateAllosteric RegulationBacterial ProteinsMutant ProteinsMycobacterium tuberculosisRho FactorRNA, Double-StrandedRNA HelicasesAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsMutant ProteinsRho FactorRNA, Double-StrandedRNA Helicases

Identifiers

PMID25999346
PMCPMC4499133
OpenAlexW1912250379

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.