ArticleThe EMBO journal2009
Conformational changes in switch I of EF-G drive its directional cycling on and off the ribosome.
Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 34 citations in OpenAlex.
- Proteotoxic Stress Bioreporter Enables Mechanism-Informed Antibiotic Discovery.Journal of natural products · 2026Article
- Structural studies of nedicistrovirus IRES-driven, initiation factor-independent translation shed light on key steps of eukaryotic translation elongation.Nucleic acids research · 2026Article
- Structural Studies of Nedicistrovirus IRES-Driven, Initiation Factor-independent Translation Shed Light on Key Steps of Eukaryotic Translation Elongation.bioRxiv : the preprint server for biology · 2025Article
- Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.Nature communications · 2021Article
- Optimization of a fluorescent-mRNA based real-time assay for precise kinetic measurements of ribosomal translocation.RNA biology · 2021Article
- Structural basis of elongation factor 2 switching.Current research in structural biology · 2020Article
- The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.Nucleic acids research · 2018Article
- Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function.RNA biology · 2016Review
- Elongation factor G initiates translocation through a power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- EF-G Activation by Phosphate Analogs.Journal of molecular biology · 2016Article
- Article
- Following movement of domain IV of elongation factor G during ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Highly conserved base A55 of 16S ribosomal RNA is important for the elongation cycle of protein synthesis.Biochemistry · 2013Article
- Control of ribosomal subunit rotation by elongation factor G.Science (New York, N.Y.) · 2013Article
- Article
- Functional role of the sarcin-ricin loop of the 23S rRNA in the elongation cycle of protein synthesis.Journal of molecular biology · 2012Article
- Archaeal ribosomal stalk protein interacts with translation factors in a nucleotide-independent manner via its conserved C terminus.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.Scientific reports · 2012Article
- A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation.The Journal of biological chemistry · 2011Article
- mRNA translocation occurs during the second step of ribosomal intersubunit rotation.Nature structural & molecular biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have trapped elongation factor G (EF-G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA-mRNA translocation in the ribosome. By probing EF-G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by approximately 20 A), relative to the 70S ribosome, during the EF-G cycle. In free EF-G, sw1 is disordered, particularly in GDP-bound and nucleotide-free states. On EF-G*GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF-G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF-G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF-G cycle during protein synthesis.
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.