ArticleMolecular microbiology2008
Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis.
Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 57 citations in OpenAlex.
- Potential Effects of Gut Microbiota in the Acute and Chronic Toxicity of Silver Nanoparticles toEnvironment & health (Washington, D.C.) · 2026Article
- A family of RRM-1 RNA binding proteins enables cold adaptation and environmental resilience inbioRxiv : the preprint server for biology · 2026Article
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- Contribution of an alternative 16S rRNA helix to biogenesis of the 30S subunit of the ribosome.RNA (New York, N.Y.) · 2024Article
- Morphological and physiological adaptations of psychrophilic Pseudarthrobacter psychrotolerans YJ56 under temperature stress.Scientific reports · 2023Article
- Roles of the leader-trailer helix and antitermination complex in biogenesis of the 30S ribosomal subunit.Nucleic acids research · 2023Article
- From Nucleus to Membrane: A Subcellular Map of the N-Acetylation Machinery in Plants.International journal of molecular sciences · 2022Review
- Ribosomal protein S18 acetyltransferase RimI is responsible for the acetylation of elongation factor Tu.The Journal of biological chemistry · 2022Article
- Protein Assistants of Small Ribosomal Subunit Biogenesis in Bacteria.Microorganisms · 2022Review
- Protein N-terminal acylation: An emerging field in bacterial cell physiology.Current trends in microbiology · 2022Article
- Quantitative Genetic Screens for Mapping Bacterial Pathways and Functional Networks.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- A Thermosensitive, Phase-Variable Epigenetic Switch:Microbiology and molecular biology reviews : MMBR · 2020Review
- RsmG forms stable complexes with premature small subunit rRNA during bacterial ribosome biogenesis.RSC advances · 2020Article
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions.Frontiers in microbiology · 2019Review
- Ribosomal background of the Bacillus cereus group thermotypes.Scientific reports · 2017Article
- The Loop 2 Region of Ribosomal Protein uS5 Influences Spectinomycin Sensitivity, Translational Fidelity, and Ribosome Biogenesis.Antimicrobial agents and chemotherapy · 2017Article
- Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.Biochemistry · 2016Review
- Review
- The large ribosomal subunit protein L9 enables the growth of EF-P deficient cells and enhances small subunit maturation.PloS one · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
A specific mutation of Escherichia coli ribosomal protein S5, in which glycine is changed to aspartate at position 28 [S5(G28D)], results in cold sensitivity and defects in ribosome biogenesis and translational fidelity. In an attempt to understand the roles of S5 in these essential cellular functions, we selected extragenic suppressors and identified rimJ as a high-copy suppressor of the cold-sensitive phenotype associated with the S5(G28D) mutation. Our studies indicate that RimJ overexpression suppresses the growth defects, anomalous ribosome profiles and mRNA misreading exhibited by the S5(G28D) mutant strain. Although previously characterized as the N-acetyltransferase of S5, our data indicate that RimJ, when devoid of acetyltransferase activity, can suppress S5(G28D) defects thus indicating that the suppression activity of RimJ is not dependent on its acetyltransferase activity. Additionally, RimJ appears to associate with pre-30S subunits indicating that it acts on the ribonucleoprotein particle. These findings suggest that RimJ has evolved dual functionality; it functions in r-protein acetylation and as a ribosome assembly factor in E. coli.
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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.