Evidence map›Paper›PMID 22002225›Full record

ArticleNature structural & molecular biology2011

Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNAi(Met) ternary complex binding to the 40S ribosome.

Byung-Sik Shin, Joo-Ran Kim, Sarah E Walker, Jinsheng Dong, Jon R Lorsch, Thomas E Dever

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. In-feedFrontiers in physiology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Stem cells international · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Upregulation of eIF5B controls cell-cycle arrest and specific developmental stages.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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 3 institutions in 1 country.

Byung-Sik ShinLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, USA.
Joo-Ran Kim
Sarah E Walker
Jinsheng Dong
Jon R Lorsch
Thomas E Dever
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USJohns Hopkins University · USNational Institutes of Health · US

Funding

Mechanism and Regulation of Eukaryotic Protein SynthesisZIAHD001010 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DEVER, THOMAS E · 2009 to 2025
$29.4M
KINETIC DISSECTION OF EUKARYOTIC TRANSLATION INITIATIONR01GM062128 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2000 to 2013
$4.6M
Intramural NIH HHS ZIA HD001010NIGMS NIH HHS GM62128NIGMS NIH HHS R01 GM062128
6 · The paper itself

Abstract

In contrast to prokaryotic elongation factor EF-Tu, which delivers aminoacyl-tRNAs to the ribosomal A-site, eukaryotic initiation factor eIF2 binds methionyl initiator transfer RNA (Met-tRNA(i)(Met)) to the P-site of the 40S ribosomal subunit. The results of directed hydroxyl radical probing experiments to map binding of Saccharomyces cerevisiae eIF2 on the ribosome and on Met-tRNA(i)(Met) revealed that eIF2γ primarily contacts the acceptor stem of Met-tRNA(i)(Met) and identified a key binding interface between domain III of eIF2γ and 18S rRNA helix h44 on the 40S subunit. Whereas the analogous domain III of EF-Tu contacts the T stem of tRNAs, biochemical analyses demonstrated that eIF2γ domain III is important for ribosome, not Met-tRNA(i)(Met). Thus, despite their structural similarity, eIF2 and EF-Tu bind tRNAs in substantially different manners, and we propose that the tRNA-binding domain III of EF-Tu has acquired a new ribosome-binding function in eIF2γ.

Indexed as

Archaeal ProteinsCysteineEukaryotic Initiation Factor-2Guanosine TriphosphateHydroxyl RadicalModels, MolecularMolecular Sequence DataNucleic Acid ConformationPeptide Elongation Factor TuProtein BindingProtein Structure, TertiaryRibosome Subunits, Small, EukaryoticRNA, Ribosomal, 18SRNA, Transfer, MetSaccharomyces cerevisiae ProteinsArchaeal ProteinsCysteineEukaryotic Initiation Factor-2Guanosine TriphosphateHydroxyl RadicalMet-tRNA(i)(Met)Peptide Elongation Factor TuRNA, Ribosomal, 18SRNA, Transfer, MetSaccharomyces cerevisiae Proteins

Identifiers

PMID22002225
PMCPMC3210414
OpenAlexW2072224564

What OpenQuestion holds

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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.