ArticleProceedings of the National Academy of Sciences of the United States of America2016
Elongation factor G initiates translocation through a power stroke.
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 42 papers.
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Who cites it
42 citing papers in PubMed, 91 citations in OpenAlex.
- The ribosome derives the energy to translocate and unwind mRNA from EF-G binding.Nature communications · 2025Article
- EF-G Mutations Reveal Correlation between Power Stroke and Translocation Fidelity in Protein Synthesis.bioRxiv : the preprint server for biology · 2025Article
- Photostability of organic fluorophore influenced by adjacent amino acid residues.Communications chemistry · 2025Article
- POLCAM: instant molecular orientation microscopy for the life sciences.Nature methods · 2024Article
- On the response of elongating ribosomes to forces opposing translocation.Biophysical journal · 2024Article
- Distinct signatures of gut microbiota and metabolites in primary biliary cholangitis with poor biochemical response after ursodeoxycholic acid treatment.Cell & bioscience · 2024Article
- Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Insights into translocation mechanism and ribosome evolution from cryo-EM structures of translocation intermediates of Giardia intestinalis.Nucleic acids research · 2023Article
- A model for ribosome translocation based on the alternated displacement of its subunits.European biophysics journal : EBJ · 2023Article
- Detection of immunoreactive proteins ofFrontiers in cellular and infection microbiology · 2023Article
- New Insights into the Mechanism of Antibacterial Action of Synthetic PeptideAntibiotics (Basel, Switzerland) · 2022Article
- The role of GTP hydrolysis by EF-G in ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis.mBio · 2022Article
- Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.Nature communications · 2021Article
- Structural mechanism of GTPase-powered ribosome-tRNA movement.Nature communications · 2021Article
- Ribosome as a Translocase and Helicase.Biochemistry. Biokhimiia · 2021Review
- Article
- Structural insights into mammalian mitochondrial translation elongation catalyzed by mtEFG1.The EMBO journal · 2020Article
- Review
- Translational recoding: canonical translation mechanisms reinterpreted.Nucleic acids research · 2020Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
During the translocation step of prokaryotic protein synthesis, elongation factor G (EF-G), a guanosine triphosphatase (GTPase), binds to the ribosomal PRE-translocation (PRE) complex and facilitates movement of transfer RNAs (tRNAs) and messenger RNA (mRNA) by one codon. Energy liberated by EF-G's GTPase activity is necessary for EF-G to catalyze rapid and precise translocation. Whether this energy is used mainly to drive movements of the tRNAs and mRNA or to foster EF-G dissociation from the ribosome after translocation has been a long-lasting debate. Free EF-G, not bound to the ribosome, adopts quite different structures in its GTP and GDP forms. Structures of EF-G on the ribosome have been visualized at various intermediate steps along the translocation pathway, using antibiotics and nonhydolyzable GTP analogs to block translocation and to prolong the dwell time of EF-G on the ribosome. However, the structural dynamics of EF-G bound to the ribosome have not yet been described during normal, uninhibited translocation. Here, we report the rotational motions of EF-G domains during normal translocation detected by single-molecule polarized total internal reflection fluorescence (polTIRF) microscopy. Our study shows that EF-G has a small (∼10°) global rotational motion relative to the ribosome after GTP hydrolysis that exerts a force to unlock the ribosome. This is followed by a larger rotation within domain III of EF-G before its dissociation from the ribosome.
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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.