Evidence map›Paper›PMID 24389466›Full record

ArticleNature structural & molecular biology2014

The ABC-F protein EttA gates ribosome entry into the translation elongation cycle.

Grégory Boël, Paul C Smith, Wei Ning, Michael T Englander, Bo Chen, Yaser Hashem, Anthony J Testa, Jeffrey J Fischer, Hans-Joachim Wieden, Joachim Frank and 2 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing 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

85 citing papers in PubMed.

  1. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
    Article
  2. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Chemical genetic interactions elucidate pathways controlling tuberculosis antibiotic efficacy during infection.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Grégory Boël1] Department of Biological Sciences, Columbia University, New York, New York, USA. [2] Northeast Structural Genomics Consortium, Columbia University, New York, New York, USA.
Paul C Smith1] Department of Biological Sciences, Columbia University, New York, New York, USA. [2].
Wei NingDepartment of Chemistry, Columbia University, New York, New York, USA.
Michael T Englander1] Department of Chemistry, Columbia University, New York, New York, USA. [2] Integrated Program in Cellular, Molecular and Biomedical Studies, Columbia University, Medical Center, New York, New York, USA. [3].
Bo ChenDepartment of Biological Sciences, Columbia University, New York, New York, USA.
Yaser Hashem1] Department of Biochemistry, Columbia University Medical Center, New York, New York, USA. [2] Howard Hughes Medical Institute, Columbia University Medical Center, New York, New York, USA.
Anthony J TestaDepartment of Biological Sciences, Columbia University, New York, New York, USA.
Jeffrey J Fischer1] Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta, Canada. [2].
Hans-Joachim WiedenDepartment of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta, Canada.
Joachim Frank1] Department of Biological Sciences, Columbia University, New York, New York, USA. [2] Department of Biochemistry, Columbia University Medical Center, New York, New York, USA. [3] Howard Hughes Medical Institute, Columbia University Medical Center, New York, New York, USA.
Ruben L GonzalezDepartment of Chemistry, Columbia University, New York, New York, USA.
John F Hunt1] Department of Biological Sciences, Columbia University, New York, New York, USA. [2] Northeast Structural Genomics Consortium, Columbia University, New York, New York, USA.

Funding

Sub-project 9U54GM074958 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KENNEDY, MICHAEL ALLEN · 2005 to 2009
$56.6M
University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
TRAINING PROGRAM IN MOLECULAR BIOPHYSICST32GM008281 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PALMER, ARTHUR G · 1988 to 2017
$5.4M
Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
The Structural Dynamics of Translation InitiationR01GM084288 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GONZALEZ, RUBEN L · 2009 to 2022
$4.4M
STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLYR37GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2006
$2.8M
CIHR MOP 114938Howard Hughes Medical InstituteNIGMS NIH HHS GM074958NIGMS NIH HHS GM084288NIGMS NIH HHS GM29169NIGMS NIH HHS GM55440NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM055440NIGMS NIH HHS R01 GM084288NIGMS NIH HHS R37 GM029169NIGMS NIH HHS T32 GM008281NIGMS NIH HHS U54 GM074958NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

ABC-F proteins have evaded functional characterization even though they compose one of the most widely distributed branches of the ATP-binding cassette (ABC) superfamily. Herein, we demonstrate that YjjK, the most prevalent eubacterial ABC-F protein, gates ribosome entry into the translation elongation cycle through a nucleotide-dependent interaction sensitive to ATP/ADP ratio. Accordingly, we rename this protein energy-dependent translational throttle A (EttA). We determined the crystal structure of Escherichia coli EttA and used it to design mutants for biochemical studies including enzymological assays of the initial steps of protein synthesis. These studies suggest that EttA may regulate protein synthesis in energy-depleted cells, which have a low ATP/ADP ratio. Consistently with this inference, EttA-deleted cells exhibit a severe fitness defect in long-term stationary phase. These studies demonstrate that an ABC-F protein regulates protein synthesis via a new mechanism sensitive to cellular energy status.

Indexed as

Peptide Chain Elongation, TranslationalATP-Binding Cassette TransportersCrystallography, X-RayEscherichia coli ProteinsModels, BiologicalModels, MolecularPhylogenyProtein Structure, TertiaryRibosomesATP-Binding Cassette TransportersEscherichia coli ProteinsEttA protein, E coli

Identifiers

PMID24389466
PMCPMC4101993

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Registered trials

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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.