Evidence map›Paper›PMID 19595714›Full record

ArticleMolecular cell2009

GTP hydrolysis by IF2 guides progression of the ribosome into elongation.

R Andrew Marshall, Colin Echeverría Aitken, Joseph D Puglisi

Abstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–field-weighted citation impact
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

60 citing papers in PubMed.

  1. Article
  2. Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Article
  4. Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. Early divergence of translation initiation and elongation factors.Protein science : a publication of the Protein Society · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Ribosome as a Translocase and Helicase.Biochemistry. Biokhimiia · 2021
    Review
  11. Article
  12. Article
  13. Single-Molecule Fluorescence Applied to Translation.Cold Spring Harbor perspectives in biology · 2019
    Review
  14. Article
  15. Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  16. Review
  17. Complementary charge-based interaction between the ribosomal-stalk protein L7/12 and IF2 is the key to rapid subunit association.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Review
  19. Article
  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

3 authors.

R Andrew MarshallDepartment of Chemistry, Stanford University, Stanford, CA 94305-5126, USA.
Colin Echeverría Aitken
Joseph D Puglisi

Funding

STRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7M
NIGMS NIH HHS R01 GM051266
6 · The paper itself

Abstract

Recent structural data have revealed two distinct conformations of the ribosome during initiation. We employed single-molecule fluorescence methods to probe the dynamic relation of these ribosomal conformations in real time. In the absence of initiation factors, the ribosome assembles in two distinct conformations. The initiation factors guide progression of the ribosome to the conformation that can enter the elongation cycle. In particular, IF2 both accelerates the rate of subunit joining and actively promotes the transition to the elongation-competent conformation. Blocking GTP hydrolysis by IF2 results in 70S complexes formed in the conformation unable to enter elongation. We observe that rapid GTP hydrolysis by IF2 drives the transition to the elongation-competent conformation, thus committing the ribosome to enter the elongation cycle.

Indexed as

CarbocyaninesEukaryotic Initiation Factor-2Fluorescence Resonance Energy TransferGuanosine TriphosphateHydrolysisKineticsModels, MolecularPeptide Chain Initiation, TranslationalPeptide Initiation FactorsProkaryotic Initiation Factor-2Protein BindingProtein ConformationRibosomesRNA, MessengerRNA, TransferCarbocyaninescyanine dye 3cyanine dye 5Eukaryotic Initiation Factor-2Guanosine TriphosphatePeptide Initiation FactorsProkaryotic Initiation Factor-2RNA, MessengerRNA, Transfer

Identifiers

PMID19595714
PMCPMC4447082

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.