ArticleProceedings of the National Academy of Sciences of the United States of America2016
Elongation factor 4 remodels the A-site tRNA on the ribosome.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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.
Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- The Conserved GTPase LepA May Contribute to the Final Proper Stabilization of the 3' Domain of the 30S Subunit During Ribosome Assembly.International journal of molecular sciences · 2026Article
- Evolution of ribosome X-ray crystallography: from first crystals to atomic resolution.Biophysical reviews · 2025Review
- Emerging mechanisms of human mitochondrial translation regulation.Trends in biochemical sciences · 2025Review
- The ribosome termination complex remodels release factor RF3 and ejects GDP.Nature structural & molecular biology · 2024Article
- Bacterial Ribosome Rescue Systems.Microorganisms · 2022Review
- In silico analysis of bacterial translation factors reveal distinct translation event specific pI values.BMC genomics · 2021Article
- The conserved translation factor LepA is required for optimal synthesis of a porin family inJournal of bacteriology · 2020Article
- Cryo-electron microscopy visualization of a large insertion in the 5S ribosomal RNA of the extremely halophilic archaeon Halococcus morrhuae.FEBS open bio · 2020Article
- Structural basis for ribosome recycling by RRF and tRNA.Nature structural & molecular biology · 2020Article
- Ribosome Structure, Function, and Early Evolution.International journal of molecular sciences · 2018Review
- Translation Elongation Factor 4 (LepA) Contributes to Tetracycline Susceptibility by Stalling Elongating Ribosomes.Antimicrobial agents and chemotherapy · 2018Article
- Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function.Molecular and cellular biology · 2017Review
- Conserved GTPase LepA (Elongation Factor 4) functions in biogenesis of the 30S subunit of the 70S ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function.RNA biology · 2016Review
- EF4 reveals the energy barrier for tRNA back-translocation in the peptidyl transferase center.RNA biology · 2016Article
- Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome.The Journal of biological chemistry · 2016Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
During translation, a plethora of protein factors bind to the ribosome and regulate protein synthesis. Many of those factors are guanosine triphosphatases (GTPases), proteins that catalyze the hydrolysis of guanosine 5'-triphosphate (GTP) to promote conformational changes. Despite numerous studies, the function of elongation factor 4 (EF-4/LepA), a highly conserved translational GTPase, has remained elusive. Here, we present the crystal structure at 2.6-Å resolution of the Thermus thermophilus 70S ribosome bound to EF-4 with a nonhydrolyzable GTP analog and A-, P-, and E-site tRNAs. The structure reveals the interactions of EF-4 with the A-site tRNA, including contacts between the C-terminal domain (CTD) of EF-4 and the acceptor helical stem of the tRNA. Remarkably, EF-4 induces a distortion of the A-site tRNA, allowing it to interact simultaneously with EF-4 and the decoding center of the ribosome. The structure provides insights into the tRNA-remodeling function of EF-4 on the ribosome and suggests that the displacement of the CCA-end of the A-site tRNA away from the peptidyl transferase center (PTC) is functionally significant.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.