ArticleJournal of molecular biology2015
Ribosomal initiation complex-driven changes in the stability and dynamics of initiation factor 2 regulate the fidelity of translation initiation.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- 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
- Current Worldwide Trends in PediatricChildren (Basel, Switzerland) · 2023Review
- Precise tuning of bacterial translation initiation by non-equilibrium 5'-UTR unfolding observed in single mRNAs.Nucleic acids research · 2022Article
- Article
- Bayesian machine learning analysis of single-molecule fluorescence colocalization images.eLife · 2022Article
- Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.International journal of molecular sciences · 2021Article
- Multiplexed genomic encoding of non-canonical amino acids for labeling large complexes.Nature chemical biology · 2020Article
- The alarmones (p)ppGpp directly regulate translation initiation during entry into quiescence.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Coming Together: RNAs and Proteins Assemble under the Single-Molecule Fluorescence Microscope.Cold Spring Harbor perspectives in biology · 2019Review
- 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
- Precisely and Accurately Inferring Single-Molecule Rate Constants.Methods in enzymology · 2016Article
- Initiation factor 2 stabilizes the ribosome in a semirotated conformation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Directional transition from initiation to elongation in bacterial translation.Nucleic acids research · 2015Article
- Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015Review
- Roles of helix H69 of 23S rRNA in translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The emerging role of rectified thermal fluctuations in initiator aa-tRNA- and start codon selection during translation initiation.Biochimie · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Joining of the large, 50S, ribosomal subunit to the small, 30S, ribosomal subunit initiation complex (IC) during bacterial translation initiation is catalyzed by the initiation factor (IF) IF2. Because the rate of subunit joining is coupled to the IF, transfer RNA (tRNA), and mRNA codon compositions of the 30S IC, the subunit joining reaction functions as a kinetic checkpoint that regulates the fidelity of translation initiation. Recent structural studies suggest that the conformational dynamics of the IF2·tRNA sub-complex forming on the intersubunit surface of the 30S IC may play a significant role in the mechanisms that couple the rate of subunit joining to the IF, tRNA, and codon compositions of the 30S IC. To test this hypothesis, we have developed a single-molecule fluorescence resonance energy transfer signal between IF2 and tRNA that has enabled us to monitor the conformational dynamics of the IF2·tRNA sub-complex across a series of 30S ICs. Our results demonstrate that 30S ICs undergoing rapid subunit joining display a high affinity for IF2 and an IF2·tRNA sub-complex that primarily samples a single conformation. In contrast, 30S ICs that undergo slower subunit joining exhibit a decreased affinity for IF2 and/or a change in the conformational dynamics of the IF2·tRNA sub-complex. These results strongly suggest that 30S IC-driven changes in the stability of IF2 and the conformational dynamics of the IF2·tRNA sub-complex regulate the efficiency and fidelity of subunit joining during translation initiation.
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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.