Evidence map›Paper›PMID 17996252›Full record

ArticleJournal of molecular biology2007

Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits.

Ning Gao, Andrey V Zavialov, Måns Ehrenberg, Joachim Frank

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

23 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Structural basis for ribosome recycling by RRF and tRNA.Nature structural & molecular biology · 2020
    Article
  9. Joachim Frank's Binding with the Ribosome.Structure (London, England : 1993) · 2019
    Review
  10. Review
  11. Article
  12. 70S-scanning initiation is a novel and frequent initiation mode of ribosomal translation in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Mechanism of eIF6 release from the nascent 60S ribosomal subunit.Nature structural & molecular biology · 2015
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  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

4 authors at 2 institutions in 1 country.

Ning GaoHoward Hughes Medical Institute, Wadsworth Center, Empire State Plaza, Albany, NY 12201-0509, USA.
Andrey V Zavialov
Måns Ehrenberg
Joachim Frank
University at Albany, State University of New York · USWadsworth Center · US

Funding

ZERNIKE PHASE-CONTRAST IMAGINGP41RR001219 · NCRR · WADSWORTH CENTER · PI WAGENKNECHT, TERENCE C · 1985 to 2010
$11.1M
STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
Biochemical and Structural Analysis of the RibosomeR01GM070768 · NIGMS · UPPSALA UNIVERSITY · PI EHRENBERG, MANS P · 2004 to 2007
$775k
NCRR NIH HHS P41 RR001219NIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM055440NIGMS NIH HHS R01 GM070768NIGMS NIH HHS R01 GM29169NIGMS NIH HHS R01 GM70768
6 · The paper itself

Abstract

After termination of protein synthesis, the bacterial ribosome is split into its 30S and 50S subunits by the action of ribosome recycling factor (RRF) and elongation factor G (EF-G) in a guanosine 5'-triphosphate (GTP)-hydrolysis-dependent manner. Based on a previous cryo-electron microscopy study of ribosomal complexes, we have proposed that the binding of EF-G to an RRF-containing posttermination ribosome triggers an interdomain rotation of RRF, which destabilizes two strong intersubunit bridges (B2a and B3) and, ultimately, separates the two subunits. Here, we present a 9-A (Fourier shell correlation cutoff of 0.5) cryo-electron microscopy map of a 50S x EF-G x guanosine 5'-[(betagamma)-imido]triphosphate x RRF complex and a quasi-atomic model derived from it, showing the interaction between EF-G and RRF on the 50S subunit in the presence of the noncleavable GTP analogue guanosine 5'-[(betagamma)-imido]triphosphate. The detailed information in this model and a comparative analysis of EF-G structures in various nucleotide- and ribosome-bound states show how rotation of the RRF head domain may be triggered by various domains of EF-G. For validation of our structural model, all known mutations in EF-G and RRF that relate to ribosome recycling have been taken into account. More importantly, our results indicate a substantial conformational change in the Switch I region of EF-G, suggesting that a conformational signal transduction mechanism, similar to that employed in transfer RNA translocation on the ribosome by EF-G, translates a large-scale movement of EF-G's domain IV, induced by GTP hydrolysis, into the domain rotation of RRF that eventually splits the ribosome into subunits.

Indexed as

Amino Acid SequenceCryoelectron MicroscopyGuanosine TriphosphateHydrolysisMolecular Sequence DataPeptide Elongation Factor GProtein ConformationRibosomal ProteinsRibosomesRNA, MessengerScattering, RadiationSequence Homology, Amino AcidGuanosine TriphosphatePeptide Elongation Factor GRibosomal Proteinsribosome releasing factorRNA, Messenger

Identifiers

PMID17996252
PMCPMC2211570
OpenAlexW2019680204

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.