Evidence map›Paper›PMID 19029312›Full record

ArticleRNA (New York, N.Y.)2009

Kinetic and thermodynamic analysis of the role of start codon/anticodon base pairing during eukaryotic translation initiation.

Sarah E Kolitz, Julie E Takacs, Jon R Lorsch

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

70 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Structural basis for non-AUG translation regulation by 5MPs.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Dual Luciferase Reporter Assay in Schizosaccharomyces pombe.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  6. Article
  7. Deciphering thebioRxiv : the preprint server for biology · 2024
    Article
  8. Article
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  12. Article
  13. Review
  14. Article
  15. Article
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  17. Article
  18. Article
  19. Article
  20. Review

10 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.

Sarah E KolitzDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Julie E Takacs
Jon R Lorsch
Johns Hopkins University · US

Funding

KINETIC DISSECTION OF EUKARYOTIC TRANSLATION INITIATIONR01GM062128 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2000 to 2013
$4.6M
Small Molecule Effectors of Eukaryotic Translation Initiation Site SelectionR21DK078633 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI LORSCH, JON R. · 2007 to 2008
$446k
NIDDK NIH HHS DK078633NIDDK NIH HHS R21 DK078633NIGMS NIH HHS GM62128NIGMS NIH HHS R01 GM062128
6 · The paper itself

Abstract

Start codon recognition is a crucial event in the initiation of protein synthesis. To gain insight into the mechanism of start codon recognition in eukaryotes, we used a yeast reconstituted initiation system to isolate the step of Met-tRNA(i)*eIF2*GTP ternary complex (TC) binding to the 40S subunit. We examined the kinetics and thermodynamics of this step in the presence of base changes in the mRNA start codon and initiator methionyl tRNA anticodon, in order to investigate the effects of base pairing and sequence on the stability of the resulting 43S*mRNA complex. We observed that the formation of three base pairs, rather than their identities, was the key determinant of stability of TC binding, indicating that nothing is inherently special about the sequence AUG for this step. Surprisingly, the rate constant for TC binding to the 40S subunit was strongly codon dependent, whereas the rate constant for TC dissociation from the 43S*mRNA complex was not. The data suggest a model in which, after the initial diffusion-limited encounter of TC with the 40S subunit, the formation of three matching start codon/anticodon base pairs triggers a conformational change that locks the complex into a stable state. This induced-fit mechanism supports the proposal that initiation codon recognition by the 43S complex induces a conformational change from an open state to a closed one that arrests movement along the mRNA.

Indexed as

AnticodonBase PairingBinding SitesCodon, InitiatorEukaryotic Initiation Factor-1Eukaryotic Initiation Factor-2KineticsModels, BiologicalPeptide Chain Initiation, TranslationalProtein SubunitsRibosome Subunits, Small, EukaryoticRNA, MessengerThermodynamicsAnticodonCodon, InitiatorEukaryotic Initiation Factor-1Eukaryotic Initiation Factor-2Protein SubunitsRNA, Messenger

Identifiers

PMID19029312
PMCPMC2612769
OpenAlexW2106459512

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.