Evidence map›Paper›PMID 19029250›Full record

ArticleMolecular and cellular biology2009

rRNA suppressor of a eukaryotic translation initiation factor 5B/initiation factor 2 mutant reveals a binding site for translational GTPases on the small ribosomal subunit.

Byung-Sik Shin, Joo-Ran Kim, Michael G Acker, Kathryn N Maher, Jon R Lorsch, Thomas E Dever

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. A Novel Inhibitor of Translation Initiation Factor eIF5B inJournal of microbiology and biotechnology · 2024
    Article
  4. Article
  5. Article
  6. Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The structure and function of the eukaryotic ribosome.Cold Spring Harbor perspectives in biology · 2012
    Review
  14. Article
  15. Article
  16. 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.

Byung-Sik ShinLaboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-2427, USA.
Joo-Ran Kim
Michael G Acker
Kathryn N Maher
Jon R Lorsch
Thomas E Dever
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Institutes of Health · USJohns Hopkins Medicine · USJohns Hopkins University · 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
REGULATION OF EUKARYOTIC PROTEIN SYNTHESISZ01HD001010 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DEVER, THOMAS E · 1995 to 2008
$2.6M
Intramural NIH HHS
6 · The paper itself

Abstract

The translational GTPases promote initiation, elongation, and termination of protein synthesis by interacting with the ribosome. Mutations that impair GTP hydrolysis by eukaryotic translation initiation factor 5B/initiation factor 2 (eIF5B/IF2) impair yeast cell growth due to failure to dissociate from the ribosome following subunit joining. A mutation in helix h5 of the 18S rRNA in the 40S ribosomal subunit and intragenic mutations in domain II of eIF5B suppress the toxic effects associated with expression of the eIF5B-H480I GTPase-deficient mutant in yeast by lowering the ribosome binding affinity of eIF5B. Hydroxyl radical mapping experiments reveal that the domain II suppressors interface with the body of the 40S subunit in the vicinity of helix h5. As the helix h5 mutation also impairs elongation factor function, the rRNA and eIF5B suppressor mutations provide in vivo evidence supporting a functionally important docking of domain II of the translational GTPases on the body of the small ribosomal subunit.

Indexed as

Protein BiosynthesisAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionBase SequenceBinding SitesConserved SequenceEukaryotic Initiation Factor-2Genes, SuppressorGTP PhosphohydrolasesHistidineHydroxyl RadicalMolecular Sequence DataPeptide Elongation Factor 1Protein Structure, TertiaryRibosome Subunits, SmallEukaryotic Initiation Factor-2FUN12 protein, S cerevisiaeGTP PhosphohydrolasesHistidineHydroxyl RadicalPeptide Elongation Factor 1RNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID19029250
PMCPMC2630678
OpenAlexW2105460881

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.