ArticleProceedings of the National Academy of Sciences of the United States of America2015
Initiation factor 2 stabilizes the ribosome in a semirotated conformation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Molecular mechanism of IF1- and IF2-driven translation initiation in bacteria.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Comparing FRET Pairs that Report on Intersubunit Rotation in Bacterial Ribosomes.Journal of molecular biology · 2023Article
- Comparing FRET pairs that report on intersubunit rotation in bacterial ribosomes.bioRxiv : the preprint server for biology · 2023Article
- Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases.International journal of molecular sciences · 2023Article
- Article
- The Structural Dynamics of Translation.Annual review of biochemistry · 2022Review
- Compact IF2 allows initiator tRNA accommodation into the P site and gates the ribosome to elongation.Nature communications · 2022Article
- Specific length and structure rather than high thermodynamic stability enable regulatory mRNA stem-loops to pause translation.Nature communications · 2022Article
- Compensating Complete Loss of Signal Recognition Particle During Co-translational Protein Targeting by the Translation Speed and Accuracy.Frontiers in microbiology · 2021Article
- Extending the Spacing between the Shine-Dalgarno Sequence and P-Site Codon Reduces the Rate of mRNA Translocation.Journal of molecular biology · 2020Article
- Article
- EF-G-induced ribosome sliding along the noncoding mRNA.Science advances · 2019Article
- Article
- Ribosome Structure, Function, and Early Evolution.International journal of molecular sciences · 2018Review
- Article
- Ensemble and single-molecule FRET studies of protein synthesis.Methods (San Diego, Calif.) · 2018Article
- Three tRNAs on the ribosome slow translation elongation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria.Nature communications · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Intersubunit rotation and movement of the L1 stalk, a mobile domain of the large ribosomal subunit, have been shown to accompany the elongation cycle of translation. The initiation phase of protein synthesis is crucial for translational control of gene expression; however, in contrast to elongation, little is known about the conformational rearrangements of the ribosome during initiation. Bacterial initiation factors (IFs) 1, 2, and 3 mediate the binding of initiator tRNA and mRNA to the small ribosomal subunit to form the initiation complex, which subsequently associates with the large subunit by a poorly understood mechanism. Here, we use single-molecule FRET to monitor intersubunit rotation and the inward/outward movement of the L1 stalk of the large ribosomal subunit during the subunit-joining step of translation initiation. We show that, on subunit association, the ribosome adopts a distinct conformation in which the ribosomal subunits are in a semirotated orientation and the L1 stalk is positioned in a half-closed state. The formation of the semirotated intermediate requires the presence of an aminoacylated initiator, fMet-tRNA(fMet), and IF2 in the GTP-bound state. GTP hydrolysis by IF2 induces opening of the L1 stalk and the transition to the nonrotated conformation of the ribosome. Our results suggest that positioning subunits in a semirotated orientation facilitates subunit association and support a model in which L1 stalk movement is coupled to intersubunit rotation and/or IF2 binding.
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