Evidence map›Paper›PMID 23623685›Full record

ArticleMolecular cell2013

The mechanism of E. coli RNA polymerase regulation by ppGpp is suggested by the structure of their complex.

Yuhong Zuo, Yeming Wang, Thomas A Steitz

Abstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing 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

123 citing papers in PubMed.

  1. Article
  2. Suppressor analysis inFrontiers in microbiology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Pathophysiology of enteropathogenicJournal of veterinary science · 2022
    Review
  18. Review
  19. The extended (p)ppGpp family: New dimensions in Stress response.Current research in microbial sciences · 2021
    Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Yuhong ZuoDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Yeming Wang
Thomas A Steitz

Funding

STRUCTURES OF DNA POLYMERASES AND FUNCTIONAL COMPLEXESR01GM057510 · NIGMS · YALE UNIVERSITY · PI STEITZ, THOMAS ARTHUR · 1998 to 2013
$4.5M
Howard Hughes Medical InstituteNIGMS NIH HHS GM057510NIGMS NIH HHS R01 GM057510
6 · The paper itself

Abstract

Guanosine tetraphosphate (ppGpp) is an alarmone that enables bacteria to adapt to their environment. It has been known for years that ppGpp acts directly on RNA polymerase (RNAP) to alter the rate of transcription, but its exact target site is still under debate. Here we report a crystal structure of Escherichia coli RNAP holoenzyme in complex with ppGpp at 4.5 Å resolution. The structure reveals that ppGpp binds at an interface between the shelf and core modules on the outer surface of RNAP, away from the catalytic center and the nucleic acid binding path. Bound ppGpp connects these two pivotal modules that may restrain the opening of the RNAP cleft. A detailed mechanism of action of ppGpp is proposed in which ppGpp prevents the closure of the active center that is induced by the binding of NTP, which could slow down nucleotide addition cycles and destabilize the initial transcription complexes.

Indexed as

Binding SitesDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsGuanosine TetraphosphateProtein BindingDNA-Directed RNA PolymerasesEscherichia coli ProteinsGuanosine Tetraphosphate

Identifiers

PMID23623685
PMCPMC3677725

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Registered trials

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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.