Evidence map›Paper›PMID 27063503›Full record

ArticleJournal of molecular biology2016

EF-G Activation by Phosphate Analogs.

Enea Salsi, Elie Farah, Dmitri N Ermolenko

Abstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.3field-weighted citation impact, top 32% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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
  11. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Ribosome as a Translocase and Helicase.Biochemistry. Biokhimiia · 2021
    Review
  16. Article
  17. Article
  18. 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 at 1 institution in 1 country.

Enea SalsiDepartment of Biochemistry and Biophysics & Center for RNA Biology, School of Medicine and Dentistry, University of Rochester, Rochester, NY 14642, USA.
Elie FarahDepartment of Biochemistry and Biophysics & Center for RNA Biology, School of Medicine and Dentistry, University of Rochester, Rochester, NY 14642, USA.
Dmitri N ErmolenkoDepartment of Biochemistry and Biophysics & Center for RNA Biology, School of Medicine and Dentistry, University of Rochester, Rochester, NY 14642, USA. Electronic address: Dmitri_Ermolenko@urmc.rochester.edu.
University of Rochester · US

Funding

Structural Dynamics of TranslationR01GM099719 · NIGMS · UNIVERSITY OF ROCHESTER · PI ERMOLENKO, DMITRI · 2012 to 2020
$2.8M
NIGMS NIH HHS R01 GM099719
6 · The paper itself

Abstract

Elongation factor G (EF-G) is a universally conserved translational GTPase that promotes the translocation of tRNA and mRNA through the ribosome. EF-G binds to the ribosome in a GTP-bound form and subsequently catalyzes GTP hydrolysis. The contribution of the ribosome-stimulated GTP hydrolysis by EF-G to tRNA/mRNA translocation remains debated. Here, we show that while EF-G•GDP does not stably bind to the ribosome and induce translocation, EF-G•GDP in complex with phosphate group analogs BeF3(-) and AlF4(-) promotes the translocation of tRNA and mRNA. Furthermore, the rates of mRNA translocation induced by EF-G in the presence of GTP and a non-hydrolyzable analog of GTP, GDP•BeF3(-) are similar. Our results are consistent with the model suggesting that GTP hydrolysis is not directly coupled to mRNA/tRNA translocation. Hence, GTP binding is required to induce the activated, translocation-competent conformation of EF-G while GTP hydrolysis triggers EF-G release from the ribosome.

Indexed as

Aluminum CompoundsBoranesFluoridesGTP PhosphohydrolasesGuanosine TriphosphateHydrolysisPeptide Elongation Factor GPhosphatesProtein BiosynthesisRibosomesRNA, MessengerRNA, TransferAluminum CompoundsBoranesboron trifluorideFluoridesGTP PhosphohydrolasesGuanosine TriphosphatePeptide Elongation Factor GPhosphatesRNA, MessengerRNA, TransfertetrafluoroaluminateBeryllium fluorideEF-GGTP hydrolysismRNA translocationRibosome

Identifiers

PMID27063503
PMCPMC4884529
OpenAlexW2408578867

What OpenQuestion holds

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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.