ArticlePloS one2014
Stabilization of homoserine-O-succinyltransferase (MetA) decreases the frequency of persisters in Escherichia coli under stressful conditions.
Article in PloS one, 2014. 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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14 citing papers in PubMed, 27 citations in OpenAlex.
- Integrating multi-omics data with network modeling to characterizeJournal of bacteriology · 2026Article
- A Ratiometric pH Sensor for Gram-Positive and Gram-Negative Bacteria.Journal of the American Chemical Society · 2026Article
- Regulation of sulfur starvation-induced proteins.3 Biotech · 2025Review
- Composition and liquid-to-solid maturation of protein aggregates contribute to bacterial dormancy development and recovery.Nature communications · 2025Article
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- Targeting Superoxide dismutase confers enhanced Reactive Oxygen Species mediated eradication of Polymyxin B inducedAntimicrobial agents and chemotherapy · 2023Article
- MetA is a "thermal fuse" that inhibits growth and protects Escherichia coli at elevated temperatures.Cell reports · 2022Article
- Article
- Protein Aggregation as a Bacterial Strategy to Survive Antibiotic Treatment.Frontiers in molecular biosciences · 2021Review
- A Quantitative Survey of Bacterial Persistence in the Presence of Antibiotics: Towards Antipersister Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2020Article
- Article
- Protein aggregation in bacteria.FEMS microbiology reviews · 2020Review
- Stationary phase persister formation in Escherichia coli can be suppressed by piperacillin and PBP3 inhibition.BMC microbiology · 2019Article
- Article
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2 authors at 1 institution in 1 country.
Funding
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Abstract
Bacterial persisters are a small subpopulation of cells that exhibit multi-drug tolerance without genetic changes. Generally, persistence is associated with a dormant state in which the microbial cells are metabolically inactive. The bacterial response to unfavorable environmental conditions (heat, oxidative, acidic stress) induces the accumulation of aggregated proteins and enhances formation of persister cells in Escherichia coli cultures. We have found that methionine supplementation reduced the frequency of persisters at mild (37°C) and elevated (42°C) temperatures, as well as in the presence of acetate. Homoserine-o-succinyltransferase (MetA), the first enzyme in the methionine biosynthetic pathway, is prone to aggregation under many stress conditions, resulting in a methionine limitation in E. coli growth. Overexpression of MetA induced the greatest number of persisters at 42°C, which is correlated to an increased level of aggregated MetA. Substitution of the native metA gene on the E. coli K-12 WE chromosome by a mutant gene encoding the stabilized MetA led to reduction in persisters at the elevated temperature and in the presence of acetate, as well as lower aggregation of the mutated MetA. Decreased persister formation at 42°C was confirmed also in E. coli K-12 W3110 and a fast-growing WErph+ mutant harboring the stabilized MetA. Thus, this is the first study to demonstrate manipulation of persister frequency under stressful conditions by stabilization of a single aggregation-prone protein, MetA.
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