ArticleNucleic acids research2019
Ribosome assembly defects subvert initiation Factor3 mediated scrutiny of bona fide start signal.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Compensatory evolution facilitates loss of prfB autoregulation in Pseudomonas fluorescens SBW25.Molecular biology and evolution · 2026Article
- Mechanistic insights into E. coli recovery from growth arrest.Nature communications · 2026Article
- Mechanistic insights intobioRxiv : the preprint server for biology · 2026Article
- DNA aptamer AptScientific reports · 2025Article
- The phenotypic spectrum ofJIMD reports · 2024Article
- Contribution of an alternative 16S rRNA helix to biogenesis of the 30S subunit of the ribosome.RNA (New York, N.Y.) · 2024Article
- Roles of the leader-trailer helix and antitermination complex in biogenesis of the 30S ribosomal subunit.Nucleic acids research · 2023Article
- Initiation at AUGUG and GUGUG sequences can lead to translation of overlapping reading frames in E. coli.Nucleic acids research · 2023Article
- Ribosome profiling enhances understanding of mycobacterial translation.Frontiers in microbiology · 2022Review
- Review
- Article
- RbfA and IF3 couple ribosome biogenesis and translation initiation to increase stress tolerance.Nucleic acids research · 2020Article
- Are Antisense Proteins in Prokaryotes Functional?Frontiers in molecular biosciences · 2020Article
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Authors and funding
2 authors.
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Abstract
In bacteria, the assembly factors tightly orchestrate the maturation of ribosomes whose competency for protein synthesis is validated by translation machinery at various stages of translation cycle. However, what transpires to the quality control measures when the ribosomes are produced with assembly defects remains enigmatic. In Escherichia coli, we show that 30S ribosomes that harbour assembly defects due to the lack of assembly factors such as RbfA and KsgA display suboptimal initiation codon recognition and bypass the critical codon-anticodon proofreading steps during translation initiation. These premature ribosomes on entering the translation cycle compromise the fidelity of decoding that gives rise to errors during initiation and elongation. We show that the assembly defects compromise the binding of initiation factor 3 (IF3), which in turn appears to license the rapid transition of 30S (pre) initiation complex to 70S initiation complex by tempering the validation of codon-anticodon interaction during translation initiation. This suggests that the premature ribosomes harbouring the assembly defects subvert the IF3 mediated proofreading of cognate initiation codon to enter the translation cycle.
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