Evidence map›Paper›PMID 21976682›Full record

ArticleThe Journal of biological chemistry2011

Tagetitoxin inhibits RNA polymerase through trapping of the trigger loop.

Irina Artsimovitch, Vladimir Svetlov, Sondra Maureen Nemetski, Vitaly Epshtein, Timothy Cardozo, Evgeny Nudler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Total Synthesis of Tagetitoxin.Journal of the American Chemical Society · 2020
    Article
  4. Review
  5. Article
  6. Review
  7. Bacterial Transcription as a Target for Antibacterial Drug Development.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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

6 authors at 2 institutions in 1 country.

Irina ArtsimovitchDepartment of Microbiology and the Center for RNA Biology, Ohio State University, Columbus, Ohio 43210, USA. artsimovitch.1@osu.edu
Vladimir Svetlov
Sondra Maureen Nemetski
Vitaly Epshtein
Timothy Cardozo
Evgeny Nudler
New York University · USThe Ohio State University · US

Funding

Mechnanism of transcript elongation control by RfaHR01GM067153 · NIGMS · OHIO STATE UNIVERSITY · PI IRINA ARTSIMOVITCH · 2003 to 2026
$8.0M
Chemical Biology Design For MalariaDP2OD004631 · OD · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI CARDOZO, TIMOTHY J · 2008 to 2014
$3.1M
A Chemical Biology Network for Personalized MedicineRC2LM010994 · NLM · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI CARDOZO, TIMOTHY J, MA'AYAN, AVI · 2010 to 2010
$2.1M
NIH HHS DP2 OD004631NLM NIH HHS RC2 LM010994
6 · The paper itself

Abstract

Tagetitoxin (Tgt) inhibits multisubunit chloroplast, bacterial, and some eukaryotic RNA polymerases (RNAPs). A crystallographic structure of Tgt bound to bacterial RNAP apoenzyme shows that Tgt binds near the active site but does not explain why Tgt acts only at certain sites. To understand the Tgt mechanism, we constructed a structural model of Tgt bound to the transcription elongation complex. In this model, Tgt interacts with the β' subunit trigger loop (TL), stabilizing it in an inactive conformation. We show that (i) substitutions of the Arg residue of TL contacted by Tgt confer resistance to inhibitor; (ii) Tgt inhibits RNAP translocation, which requires TL movements; and (iii) paused complexes and a "slow" enzyme, in which the TL likely folds into an altered conformation, are resistant to Tgt. Our studies highlight the role of TL as a target through which accessory proteins and antibiotics can alter the elongation complex dynamics.

Indexed as

Bacterial ProteinsDNA-Directed RNA PolymerasesModels, MolecularDicarboxylic AcidsOrganophosphorus CompoundsProtein Structure, SecondaryThermus thermophilusBacterial ProteinsDicarboxylic AcidsDNA-Directed RNA PolymerasesOrganophosphorus Compoundstagetitoxin

Identifiers

PMID21976682
PMCPMC3220573
OpenAlexW2009876395

What OpenQuestion holds

Textmetadata
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.