Evidence map›Paper›PMID 23893413›Full record

ArticleThe Journal of biological chemistry2013

β-Hairpin loop of eukaryotic initiation factor 1 (eIF1) mediates 40 S ribosome binding to regulate initiator tRNA(Met) recruitment and accuracy of AUG selection in vivo.

Pilar Martin-Marcos, Jagpreet Nanda, Rafael E Luna, Gerhard Wagner, Jon R Lorsch, Alan G Hinnebusch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.8field-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

38 citing papers in PubMed, 52 citations in OpenAlex.

  1. Structural basis for non-AUG translation regulation by 5MPs.bioRxiv : the preprint server for biology · 2025
    Article
  2. eIF1 and eIF5 dynamically control translation start site fidelity.Nature structural & molecular biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Inhibitors of eIF4G1-eIF1 uncover its regulatory role of ER/UPR stress-response genes independent of eIF2α-phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Translation Phases in Eukaryotes.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Crystal structure of the C-terminal domain of DENR.Computational and structural biotechnology journal · 2020
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018
    Review
  20. 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 4 institutions in 1 country.

Pilar Martin-MarcosLaboratory of Gene Regulation and Development, Eunice K. Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.
Jagpreet NandaDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Rafael E LunaDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Jon R LorschDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205. Electronic address: jlorsch@jhmi.edu.
Alan G HinnebuschLaboratory of Gene Regulation and Development, Eunice K. Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892. Electronic address: ahinnebusch@nih.gov.
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USHarvard University · USJohns Hopkins Medicine · USJohns Hopkins University · US

Funding

Translational & Transcriptional Control Of Gene Expression By Nutrients In YeastZIAHD001004 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI HINNEBUSCH, ALAN G · 2009 to 2025
$34.4M
KINETIC DISSECTION OF EUKARYOTIC TRANSLATION INITIATIONR01GM062128 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2000 to 2013
$4.6M
STRUCTURAL BASIS OF TRANSLATION INITIATION BY EIF-4ER01CA068262 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2015
$3.6M
Intramural NIH HHSNCI NIH HHS CA068262NCI NIH HHS R01 CA068262NIGMS NIH HHS GM62128NIGMS NIH HHS R01 GM062128
6 · The paper itself

Abstract

Recognition of the translation initiation codon is thought to require dissociation of eIF1 from the 40 S ribosomal subunit, enabling irreversible GTP hydrolysis (Pi release) by the eIF2·GTP·Met-tRNAi ternary complex (TC), rearrangement of the 40 S subunit to a closed conformation incompatible with scanning, and stable binding of Met-tRNAi to the P site. The crystal structure of a Tetrahymena 40 S·eIF1 complex revealed several basic amino acids in eIF1 contacting 18 S rRNA, and we tested the prediction that their counterparts in yeast eIF1 are required to prevent premature eIF1 dissociation from scanning ribosomes at non-AUG triplets. Supporting this idea, substituting Lys-60 in helix α1, or either Lys-37 or Arg-33 in β-hairpin loop-1, impairs binding of yeast eIF1 to 40 S·eIF1A complexes in vitro, and it confers increased initiation at UUG codons (Sui(-) phenotype) or lethality, in a manner suppressed by overexpressing the mutant proteins or by an eIF1A mutation (17-21) known to impede eIF1 dissociation in vitro. The eIF1 Sui(-) mutations also derepress translation of GCN4 mRNA, indicating impaired ternary complex loading, and this Gcd(-) phenotype is likewise suppressed by eIF1 overexpression or the 17-21 mutation. These findings indicate that direct contacts of eIF1 with 18 S rRNA seen in the Tetrahymena 40 S·eIF1 complex are crucial in yeast to stabilize the open conformation of the 40 S subunit and are required for rapid TC loading and ribosomal scanning and to impede rearrangement to the closed complex at non-AUG codons. Finally, we implicate the unstructured N-terminal tail of eIF1 in blocking rearrangement to the closed conformation in the scanning preinitiation complex.

Indexed as

Basic-Leucine Zipper Transcription FactorsCodon, InitiatorEukaryotic Initiation Factor-1MutationPeptide Chain Initiation, TranslationalProtein Structure, SecondaryProtein Structure, TertiaryProtozoan ProteinsRibosome Subunits, Small, EukaryoticRNA, FungalRNA, MessengerRNA, Transfer, MetSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTetrahymena thermophilaBasic-Leucine Zipper Transcription FactorsCodon, InitiatorEukaryotic Initiation Factor-1GCN4 protein, S cerevisiaeProtozoan ProteinsRNA, FungalRNA, MessengerRNA, Transfer, MetSaccharomyces cerevisiae ProteinsSUI1 protein, S cerevisiaeAUG RecognitioneIF1eIF2Ribosome FunctionRibosomesTransfer RNA (tRNA)TranslationTranslation Initiation Factors

Identifiers

PMID23893413
PMCPMC3779751
OpenAlexW2083211507

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.