Evidence map›Paper›PMID 22605777›Full record

ArticleScience (New York, N.Y.)2012

How hibernation factors RMF, HPF, and YfiA turn off protein synthesis.

Yury S Polikanov, Gregor M Blaha, Thomas A Steitz

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

153 citing papers in PubMed, 229 citations in OpenAlex.

  1. Article
  2. Distinctive Lacritin Cleavage-Potentiated Bactericidal Alteration of thebioRxiv : the preprint server for biology · 2026
    Article
  3. Ribosome hibernation in zinc-starvedMicrobiology spectrum · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

93 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

3 authors at 1 institution in 1 country.

Yury S PolikanovDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
Gregor M Blaha
Thomas A Steitz
Yale University · US

Funding

X-RAY ANALYSIS OF PROTEIN STRUCTURE AND FUNCTIONP01GM022778 · NIGMS · YALE UNIVERSITY · PI BREAKER, RONALD R · 1985 to 2019
$26.1M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Howard Hughes Medical InstituteNIBIB NIH HHS P30 EB009998NIGMS NIH HHS GM022778NIGMS NIH HHS P01 GM022778
6 · The paper itself

Abstract

Eubacteria inactivate their ribosomes as 100S dimers or 70S monomers upon entry into stationary phase. In Escherichia coli, 100S dimer formation is mediated by ribosome modulation factor (RMF) and hibernation promoting factor (HPF), or alternatively, the YfiA protein inactivates ribosomes as 70S monomers. Here, we present high-resolution crystal structures of the Thermus thermophilus 70S ribosome in complex with each of these stationary-phase factors. The binding site of RMF overlaps with that of the messenger RNA (mRNA) Shine-Dalgarno sequence, which prevents the interaction between the mRNA and the 16S ribosomal RNA. The nearly identical binding sites of HPF and YfiA overlap with those of the mRNA, transfer RNA, and initiation factors, which prevents translation initiation. The binding of RMF and HPF, but not YfiA, to the ribosome induces a conformational change of the 30S head domain that promotes 100S dimer formation.

Indexed as

Bacterial ProteinsBinding SitesCrystallography, X-RayEscherichia coli ProteinsModels, MolecularPeptide Chain Initiation, TranslationalProkaryotic Initiation FactorsProtein BindingProtein ConformationProtein Structure, TertiaryRibosomal ProteinsRibosomesRibosome Subunits, Small, BacterialRNA, BacterialRNA, MessengerRNA, Ribosomal, 16SBacterial ProteinsEscherichia coli ProteinsHPF protein, E coliProkaryotic Initiation FactorsRaiA protein, E coliRibosomal Proteinsribosome modulation factor, E coliRNA, BacterialRNA, MessengerRNA, Ribosomal, 16SRNA, Transfer

Identifiers

PMID22605777
PMCPMC3377384
OpenAlexW2159713856

What OpenQuestion holds

Textmetadata
LicenceTDM
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.