Evidence map›Paper›PMID 24324168›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Visualization of two transfer RNAs trapped in transit during elongation factor G-mediated translocation.

David J F Ramrath, Laura Lancaster, Thiemo Sprink, Thorsten Mielke, Justus Loerke, Harry F Noller, Christian M T Spahn

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

97 citing papers in PubMed, 138 citations in OpenAlex.

  1. eLife · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Staph wars: the antibiotic pipeline strikes back.Microbiology (Reading, England) · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. The role of GTP hydrolysis by EF-G in ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  18. The cyclic octapeptide antibiotic argyrin B inhibits translation by trapping EF-G on the ribosome during translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Review

37 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

7 authors at 3 institutions in 2 countries.

David J F RamrathInstitut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, 10117-Berlin, Germany.
Laura Lancaster
Thiemo Sprink
Thorsten Mielke
Justus Loerke
Harry F Noller
Christian M T Spahn
Charité - Universitätsmedizin Berlin · DEUniversity of California, Santa Cruz · USMax Planck Institute for Molecular Genetics · DE

Funding

CRYSTAL STRUCTURE OF THE RIBOSOMER01GM059140 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1999 to 2015
$7.2M
RIBOSOME STRUCTURE AND FUNCTIONR01GM017129 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1985 to 2015
$6.9M
RIBOSOME STRUCTURE AND FUNCTIONR37GM017129 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1990 to 1999
–
NIGMS NIH HHS GM-17129NIGMS NIH HHS GM-59140NIGMS NIH HHS R01 GM017129NIGMS NIH HHS R01 GM059140NIGMS NIH HHS R37 GM017129
6 · The paper itself

Abstract

During protein synthesis, coupled translocation of messenger RNAs (mRNA) and transfer RNAs (tRNA) through the ribosome takes place following formation of each peptide bond. The reaction is facilitated by large-scale conformational changes within the ribosomal complex and catalyzed by elongtion factor G (EF-G). Previous structural analysis of the interaction of EF-G with the ribosome used either model complexes containing no tRNA or only a single tRNA, or complexes where EF-G was directly bound to ribosomes in the posttranslocational state. Here, we present a multiparticle cryo-EM reconstruction of a translocation intermediate containing two tRNAs trapped in transit, bound in chimeric intrasubunit ap/P and pe/E hybrid states. The downstream ap/P-tRNA is contacted by domain IV of EF-G and P-site elements within the 30S subunit body, whereas the upstream pe/E-tRNA maintains tight interactions with P-site elements of the swiveled 30S head. Remarkably, a tight compaction of the tRNA pair can be seen in this state. The translocational intermediate presented here represents a previously missing link in understanding the mechanism of translocation, revealing that the ribosome uses two distinct molecular ratchets, involving both intra- and intersubunit rotational movements, to drive the synchronous movement of tRNAs and mRNA.

Indexed as

Models, MolecularNucleic Acid ConformationCryoelectron MicroscopyCrystallography, X-RayEscherichia coliImage Processing, Computer-AssistedPeptide Chain Elongation, TranslationalPeptide Elongation Factor GRibosomesRNA, MessengerRNA, TransferPeptide Elongation Factor GRNA, MessengerRNA, Transferchimeric hybrid statefusidic acidratchetingribosome dynamicstranslocation mechanism

Identifiers

PMID24324168
PMCPMC3876219
OpenAlexW1984043400

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.