ArticleJournal of molecular biology2015
Translation initiation factor 3 regulates switching between different modes of ribosomal subunit joining.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- A Standardized Prism-Based TIRF Platform for Quantitative Single-Molecule Fluorescence Studies of Biomolecular Dynamics.Biosensors · 2026Article
- Mechanistic insights into E. coli recovery from growth arrest.Nature communications · 2026Article
- Mechanistic insights intobioRxiv : the preprint server for biology · 2026Article
- Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.Nucleic acids research · 2025Article
- The mechanism of mRNA cap recognition.Nature · 2025Article
- The mechanism of mRNA activation.bioRxiv : the preprint server for biology · 2023Article
- Entropic control of the free-energy landscape of an archetypal biomolecular machine.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The initiation factor 3 (IF3) residues interacting with initiator tRNA elbow modulate the fidelity of translation initiation and growth fitness in Escherichia coli.Nucleic acids research · 2022Article
- Precise tuning of bacterial translation initiation by non-equilibrium 5'-UTR unfolding observed in single mRNAs.Nucleic acids research · 2022Article
- Insights into genome recoding from the mechanism of a classic +1-frameshifting tRNA.Nature communications · 2021Article
- Article
- Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Ensemble and single-molecule FRET studies of protein synthesis.Methods (San Diego, Calif.) · 2018Article
- IF2 and unique features of initiator tRNARNA biology · 2018Article
- A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria.Nature communications · 2017Article
- Stochastic dynamics of genetic broadcasting networks.Physical review. E · 2017Article
- Article
- Solution structure of protein synthesis initiation factor 1 from Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2016Article
- Article
- The ribosome in action: Tuning of translational efficiency and protein folding.Protein science : a publication of the Protein Society · 2016Review
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2 authors.
Funding
Abstract
Ribosomal subunit joining is a key checkpoint in the bacterial translation initiation pathway during which initiation factors (IFs) regulate association of the 30S initiation complex (IC) with the 50S subunit to control formation of a 70S IC that can enter into the elongation stage of protein synthesis. The GTP-bound form of IF2 accelerates subunit joining, whereas IF3 antagonizes subunit joining and plays a prominent role in maintaining translation initiation fidelity. The molecular mechanisms through which IF2 and IF3 collaborate to regulate the efficiency of 70S IC formation, including how they affect the dynamics of subunit joining, remain poorly defined. Here, we use single-molecule fluorescence resonance energy transfer to monitor the interactions between IF2 and the GTPase-associated center (GAC) of the 50S subunit during real-time subunit joining reactions in the absence and presence of IF3. In the presence of IF3, IF2-mediated subunit joining becomes reversible, and subunit joining events cluster into two distinct classes corresponding to formation of shorter- and longer-lifetime 70S ICs. Inclusion of IF3 within the 30S IC was also found to alter the conformation of IF2 relative to the GAC, suggesting that IF3's regulatory effects may stem in part from allosteric modulation of IF2-GAC interactions. The results are consistent with a model in which IF3 can exert control over the efficiency of subunit joining by modulating the conformation of the 30S IC, which in turn influences the formation of stabilizing intersubunit contacts and thus the reaction's degree of reversibility.
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