Polyphosphate Kinase Protects Salmonella enterica from Weak Organic Acid Stress
Open accessAbstract
Mutants of Salmonella enterica lacking polyphosphate kinase (ppk) grow poorly in the presence of the weak organic acids acetate, propionate, and benzoate. This sensitivity is corrected by methionine and seems to result from destabilization of MetA (homoserine transsuccinylase), the first enzyme in methionine biosynthesis. The MetA protein is known to be sensitive to thermal inactivation, and ppk mutants are more sensitive to heat-induced methionine auxotrophy. Peroxide increases the sensitivity of ppk mutants to both heat and acid and may oxidatively damage (carbonylate) destabilized MetA. While acid appears to impair methionine biosynthesis, it leads to derepression of MetA and may inhibit growth by causing toxic accumulation of denatured protein. This is supported by the observation that the overexpression of MetA in ppk mutants causes acid sensitivity that is not corrected by methionine. We propose that polyphosphate acts as a chemical chaperone that helps refold MetA and/or may stimulate proteolysis of toxic denatured protein. The instability of MetA protein may provide a metabolic fuse that blocks growth under conditions that denature proteins; the sensitivity of this fuse is modulated by polyphosphate.
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The inhibitory effect of acetate on bacterial growth has been associated with the destabilization of homoserine transsuccinylase, the first enzyme responsible for the biosynthesis of methionine, an essential amino acid.
“The inhibitory effect of acetate on bacterial growth has been associated with the destabilization of homoserine transsuccinylase, the first enzyme responsible for the biosynthesis of methionine, an essential amino acid [102].”
From Challenges and Opportunities to Increase Economic Feasibility and Sustainability of Mixotrophic Cultivation of Green Microalgae of the Genus Chlorella (2022) · cites this paper as [102]
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- Authors
- Price-Carter, M., Fazzio, T. G., Vallbona, E. I., & Roth, J. R.
- Affiliations
- University of Utah (US)
- Department of Biology, University of Utah, Salt Lake City, Utah 84112
- Corresponding author
- Roth, John R.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2005-05
- Volume
- 187
- Issue
- 9
- Pages
- 3088-3099
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC1082818
- OpenAlex
- W2158836491
- Cited by
- 44
- References
- 64
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 2 · 2022: 2 · 2021: 1 · 2020: 3 · 2019: 2 · 2018: 1 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 5 · 2012: 2
- FWCI
- 1.44
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Utah
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM034804, GM34804)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- polyphosphate kinase, Salmonella enterica, methionine biosynthesis, Meta, protein denaturation, chemical chaperones, polyphosphate, methionine auxotrophy, heat stress, peroxides, acetate, propionate, benzoate, protein refolding, proteolysis
- MeSH terms
- Acids, Acyltransferases, Adaptation, Physiological, Bacterial Proteins, Cloning, Molecular, Enzyme Stability, Hydrogen Peroxide, Methionine, Polyphosphates, Protein Denaturation, Sigma Factor, Mutagenesis, Insertional, Gene Deletion, Phosphotransferases (Phosphate Group Acceptor), Salmonella enterica, Homoserine O-Succinyltransferase
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