ArticleProceedings of the National Academy of Sciences of the United States of America2015
Roles of helix H69 of 23S rRNA in translation initiation.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Molecular mechanism of IF1- and IF2-driven translation initiation in bacteria.bioRxiv : the preprint server for biology · 2026Article
- The Pseudomonas aeruginosa ribonuclease Ribocin cleaves eukaryotic ribosomes at helix 69 to inhibit host translation.PLoS biology · 2026Article
- Role of the sarcin-ricin loop of 23S rRNA in biogenesis of the 50S ribosomal subunit.RNA (New York, N.Y.) · 2025Article
- Ribosomes lacking bS21 gain function to regulate protein synthesis in Flavobacterium johnsoniae.Nucleic acids research · 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
- Roles of specific aminoglycoside-ribosome interactions in the inhibition of translation.RNA (New York, N.Y.) · 2019Article
- Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- IF2 and unique features of initiator tRNARNA biology · 2018Article
- Contributions of the N- and C-Terminal Domains of Initiation Factor 3 to Its Functions in the Fidelity of Initiation and Antiassociation of the Ribosomal Subunits.Journal of bacteriology · 2017Article
- Two highly conserved features of bacterial initiator tRNAs license them to pass through distinct checkpoints in translation initiation.Nucleic acids research · 2017Article
- Intersubunit Bridges of the Bacterial Ribosome.Journal of molecular biology · 2016Review
- Initiation factor 2 stabilizes the ribosome in a semirotated conformation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Initiation of translation involves the assembly of a ribosome complex with initiator tRNA bound to the peptidyl site and paired to the start codon of the mRNA. In bacteria, this process is kinetically controlled by three initiation factors--IF1, IF2, and IF3. Here, we show that deletion of helix H69 (∆H69) of 23S rRNA allows rapid 50S docking without concomitant IF3 release and virtually eliminates the dependence of subunit joining on start codon identity. Despite this, overall accuracy of start codon selection, based on rates of formation of elongation-competent 70S ribosomes, is largely uncompromised in the absence of H69. Thus, the fidelity function of IF3 stems primarily from its interplay with initiator tRNA rather than its anti-subunit association activity. While retaining fidelity, ∆H69 ribosomes exhibit much slower rates of overall initiation, due to the delay in IF3 release and impedance of an IF3-independent step, presumably initiator tRNA positioning. These findings clarify the roles of H69 and IF3 in the mechanism of translation initiation and explain the dominant lethal phenotype of the ∆H69 mutation.
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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.