ArticleRNA (New York, N.Y.)2009
Accuracy modulating mutations of the ribosomal protein S4-S5 interface do not necessarily destabilize the rps4-rps5 protein-protein interaction.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Inactivation of the ribosome assembly factor RimP causes streptomycin resistance and impairs motility inAntimicrobial agents and chemotherapy · 2024Article
- Deficiency in ribosome biogenesis causes streptomycin resistance and impairs motility inbioRxiv : the preprint server for biology · 2024Article
- Directed evolution of rRNA improves translation kinetics and recombinant protein yield.Nature communications · 2021Article
- Review
- The C-terminus of ribosomal protein uS4 contributes to small ribosomal subunit biogenesis and the fidelity of translation.Biochimie · 2017Article
- Mutations of ribosomal protein S5 suppress a defect in late-30S ribosomal subunit biogenesis caused by lack of the RbfA biogenesis factor.RNA (New York, N.Y.) · 2015Article
- Modulation of decoding fidelity by ribosomal proteins S4 and S5.Journal of bacteriology · 2015Article
- Reorganization of an intersubunit bridge induced by disparate 16S ribosomal ambiguity mutations mimics an EF-Tu-bound state.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Specific contacts between protein S4 and ribosomal RNA are required at multiple stages of ribosome assembly.RNA (New York, N.Y.) · 2013Article
- The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy.RNA (New York, N.Y.) · 2012Article
- Missense suppressor mutations in 16S rRNA reveal the importance of helices h8 and h14 in aminoacyl-tRNA selection.RNA (New York, N.Y.) · 2010Article
- Protein-protein interactions between sigma(70) region 4 of RNA polymerase and Escherichia coli SoxS, a transcription activator that functions by the prerecruitment mechanism: evidence for "off-DNA" and "on-DNA" interactions.Journal of molecular biology · 2010Article
- Hyperaccurate and error-prone ribosomes exploit distinct mechanisms during tRNA selection.Molecular cell · 2010Article
- Appropriate maturation and folding of 16S rRNA during 30S subunit biogenesis are critical for translational fidelity.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
During the process of translation, an aminoacyl tRNA is selected in the A site of the decoding center of the small subunit based on the correct codon-anticodon base pairing. Though selection is usually accurate, mutations in the ribosomal RNA and proteins and the presence of some antibiotics like streptomycin alter translational accuracy. Recent crystallographic structures of the ribosome suggest that cognate tRNAs induce a "closed conformation" of the small subunit that stabilizes the codon-anticodon interactions at the A site. During formation of the closed conformation, the protein interface between rpS4 and rpS5 is broken while new contacts form with rpS12. Mutations in rpS12 confer streptomycin resistance or dependence and show a hyperaccurate phenotype. Mutations reversing streptomycin dependence affect rpS4 and rpS5. The canonical rpS4 and rpS5 streptomycin independent mutations increase translational errors and were called ribosomal ambiguity mutations (ram). The mutations in these proteins are proposed to affect formation of the closed complex by breaking the rpS4-rpS5 interface, which reduces the cost of domain closure and thus increases translational errors. We used a yeast two-hybrid system to study the interactions between the small subunit ribosomal proteins rpS4 and rpS5 and to test the effect of ram mutations on the stability of the interface. We found no correlation between ram phenotype and disruption of the interface.
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