ArticlemBio2022
A Conundrum of r-Protein Stability: Unbalanced Stoichiometry of r-Proteins during Stationary Phase in Escherichia coli.
Article in mBio, 2022. 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.
- Article
- Selective Reprogramming of Ribosome Assembly and Translational Control during Bacterial Growth Phase Transitions.ACS omega · 2026Article
- Single-cell heterogeneity in ribosome levels and protein synthesis during nutrient starvation is driven by cAMP signaling.Science advances · 2026Article
- Ribosome Heterogeneity Revealed by Complex-Up Native Mass Spectrometry and Top-Down Proteomics.Journal of the American Chemical Society · 2026Article
- Phase-Specific Antibiotic Resistance Mechanisms in anbioRxiv : the preprint server for biology · 2025Article
- Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts:Chemical reviews · 2025Review
- Lessons from RatA: Why the Basics in Molecular Biology Are Still Crucial!International journal of molecular sciences · 2025Article
- Ampicillin treatment in persister cell studies may cause non-physiological artifacts.Microbial cell (Graz, Austria) · 2025Article
- Ribosomal RNA modification enzymes stimulate large ribosome subunit assembly in E. coli.Nucleic acids research · 2024Article
- SILAC analysis ofMicrobiology resource announcements · 2024Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- Costs of ribosomal RNA stabilization affect ribosome composition at maximum growth rate.Communications biology · 2024Article
- Ribosome Protein Composition Mediates Translation during theInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial ribosomes are composed of three rRNA and over 50 ribosomal protein (r-protein) molecules. r-proteins are essential for ribosome assembly and structural stability and also participate in almost all ribosome functions. Ribosomal components are present in stoichiometric amounts in the mature 70S ribosomes during exponential and early stationary growth phases. Ribosomes are degraded in stationary phase; however, the stability and fate of r-proteins during stationary growth phase are not known. In this study, we report a quantitative analysis of ribosomal components during extended stationary-phase growth in Escherichia coli. We show that (i) the quantity of ribosomes per cell mass decreases in stationary phase, (ii) 70S ribosomes contain r-proteins in stoichiometric amounts, (iii) 30S subunits are degraded faster than 50S subunits, (iv) the quantities of 21 r-proteins in the total proteome decrease during 14 days (short-lived r-proteins) concomitantly with the reduction of cellular RNA, and (e) 30 r-proteins are stable and form a pool of free r-proteins (stable r-proteins). Thus, r-proteins are present in nonstoichiometric amounts in the proteome of E. coli during the extended stationary phase.
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