The Acetate Switch
Open accessAbstract
SUMMARY: To succeed, many cells must alternate between life-styles that permit rapid growth in the presence of abundant nutrients and ones that enhance survival in the absence of those nutrients. One such change in life-style, the “acetate switch,” occurs as cells deplete their environment of acetate-producing carbon sources and begin to rely on their ability to scavenge for acetate. This review explains why, when, and how cells excrete or dissimilate acetate. The central components of the “switch” (phosphotransacetylase [PTA], acetate kinase [ACK], and AMP-forming acetyl coenzyme A synthetase [AMP-ACS]) and the behavior of cells that lack these components are introduced. Acetyl phosphate (acetyl∼P), the high-energy intermediate of acetate dissimilation, is discussed, and conditions that influence its intracellular concentration are described. Evidence is provided that acetyl∼P influences cellular processes from organelle biogenesis to cell cycle regulation and from biofilm development to pathogenesis. The merits of each mechanism proposed to explain the interaction of acetyl∼P with two-component signal transduction pathways are addressed. A short list of enzymes that generate acetyl∼P by PTA-ACKA-independent mechanisms is introduced and discussed briefly. Attention is then directed to the mechanisms used by cells to “flip the switch,” the induction and activation of the acetate-scavenging AMP-ACS. First, evidence is presented that nucleoid proteins orchestrate a progression of distinct nucleoprotein complexes to ensure proper transcription of its gene. Next, the way in which cells regulate AMP-ACS activity through reversible acetylation is described. Finally, the “acetate switch” as it exists in selected eubacteria, archaea, and eukaryotes, including humans, is described.
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In many microbes, acetyl-CoA is enzymatically cleaved via phosphorolysis to yield acetyl phosphate.
“In a plethora of microbes, acetyl-CoA is enzymatically cleaved via phosphorolysis to yield acetyl phosphate [79,80], which, with its high free energy of hydrolysis (ΔG°′) of –43 kJ mol−1, can phosphorylate any number of substrates, including ADP to generate ATP, with a free energy of hydrolysis (ΔG°′) of –31 kJ mol−1.”
From Early bioenergetic evolution (2013) · cites this paper as [79]
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“In a plethora of microbes, acetyl-CoA is enzymatically cleaved via phosphorolysis to yield acetyl phosphate [79,80], which, with its high free energy of hydrolysis (DG80) of –43 kJ mol(21), can phosphorylate any number of substrates, including ADP to generate ATP, with a free energy of hydrolysis (DG80) of –31 kJ mol(…”
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- Authors
- Wolfe, A. J.
- Affiliations
- Loyola University Chicago (US)
- Corresponding author
- Wolfe, Alan J.
- ORCID
- Wolfe, Alan J.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 2005-03
- Volume
- 69
- Issue
- 1
- Pages
- 12-50
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- PMC
- PMC1082793
- OpenAlex
- W2152875113
- Cited by
- 1,233
- References
- 4
- Citations by year
- 2026: 63 · 2025: 54 · 2024: 55 · 2023: 49 · 2022: 70 · 2021: 90 · 2020: 75 · 2019: 60 · 2018: 66 · 2017: 66 · 2016: 49 · 2015: 86 · 2014: 80 · 2013: 61 · 2012: 47
- FWCI
- 4.55
- Type
- journal article
- Language
- en
- Open access
- green
- dx.doi.org
- Locations
- Microbiology and Molecular Biology Reviews (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Loyola University Chicago
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Keywords
- phosphotransacetylase, acetate kinase, acetyl coenzyme A synthetase, acetyl phosphate, two-component signal transduction, gene expression regulation, biofilm growth, cell cycle regulation, organelle biogenesis, pathogenesis, eubacteria, archaea, eukaryotes
- MeSH terms
- Acetates, Animals, Bacteria, Citric Acid Cycle, Colon, Mammals
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