Acetylation of the Chemotaxis Response Regulator CheY by Acetyl-CoA Synthetase Purified from Escherichia coli

Barak, Rina; Prasad, K. Nagendra; Shainskaya, Alla; Wolfe, Alan J.; Eisenbach, Michael

doi:10.1016/j.jmb.2004.07.020

Cited by 61 publications

(103 citation statements)

References 94 publications

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“…Clearly, some inconsistencies remain, the most pressing being the observation that the acetylϳP-dependent activation of 30 WOLFE MICROBIOL. MOL.…”

Section: How Does Acetylϳp Work?mentioning

confidence: 99%

“…The acetylated enzyme (AMP-ACS-Ac) is inactive (426), because acetylation inhibits the adenylylation of acetate (169) while the thioester-forming step remains unaffected (169,200,426). In vitro, AMP-ACS also acetylates itself, also on K609 (30). This may represent the source of the low-intensity signal observed in cells that lack PAT (425).…”

Section: Post-translational Control By Acetylation-deacetylationmentioning

confidence: 99%

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The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

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1,068

1,274

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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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“…Clearly, some inconsistencies remain, the most pressing being the observation that the acetylϳP-dependent activation of 30 WOLFE MICROBIOL. MOL.…”

Section: How Does Acetylϳp Work?mentioning

confidence: 99%

Section: Post-translational Control By Acetylation-deacetylationmentioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

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1,068

1,274

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“…The response regulator CheY, involved in bacterial chemotaxis, is predicted to be under the control of RLA (166,206). While the phosphorylation of CheY has been extensively studied, the effect of acetylation on the activity of the protein is still poorly understood (207)(208)(209).…”

Section: Rla Targets Whose Modifying Acetyltransferases Are Not Knownmentioning

confidence: 99%

“…Previously, acetylation of CheY was hypothesized to occur via either autoacetylation or acetyl-CoA synthetase-dependent acetylation by some unknown mechanism (206,211). To date, studies of CheY have been performed by chemical acetylation of the protein using acetic anhydride (208).…”

Section: Rla Targets Whose Modifying Acetyltransferases Are Not Knownmentioning

confidence: 99%

“…To date, studies of CheY have been performed by chemical acetylation of the protein using acetic anhydride (208). However, this method does not acetylate CheY to the same extent as what is seen for the protein in vivo (166,206). It is currently hypothesized that there must be a GNAT responsible for the acetylation of CheY and that it is yet to be discovered.…”

Section: Rla Targets Whose Modifying Acetyltransferases Are Not Knownmentioning

confidence: 99%

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Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel

Escalante‐Semerena

2015

Microbiol Mol Biol Rev

163

175

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SUMMARY Acylation of biomolecules (e.g., proteins and small molecules) is a process that occurs in cells of all domains of life and has emerged as a critical mechanism for the control of many aspects of cellular physiology, including chromatin maintenance, transcriptional regulation, primary metabolism, cell structure, and likely other cellular processes. Although this review focuses on the use of acetyl moieties to modify a protein or small molecule, it is clear that cells can use many weak organic acids (e.g., short-, medium-, and long-chain mono- and dicarboxylic aliphatics and aromatics) to modify a large suite of targets. Acetylation of biomolecules has been studied for decades within the context of histone-dependent regulation of gene expression and antibiotic resistance. It was not until the early 2000s that the connection between metabolism, physiology, and protein acetylation was reported. This was the first instance of a metabolic enzyme (acetyl coenzyme A [acetyl-CoA] synthetase) whose activity was controlled by acetylation via a regulatory system responsive to physiological cues. The above-mentioned system was comprised of an acyltransferase and a partner deacylase. Given the reversibility of the acylation process, this system is also referred to as r eversible l ysine a cylation (RLA). A wealth of information has been obtained since the discovery of RLA in prokaryotes, and we are just beginning to visualize the extent of the impact that this regulatory system has on cell function.

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Methylation‐independent adaptation in chemotaxis of Escherichia coli involves acetylation‐dependent speed adaptation

2017

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Chemoreceptor methylation and demethylation has been shown to be at the core of the adaptation mechanism in Escherichia coli chemotaxis. Nevertheless, mutants lacking the methylation machinery can adapt to some extent. Here we carried out an extensive quantitative analysis of chemotactic and chemokinetic methylation-independent adaptation. We show that partial or complete adaptation of the direction of flagellar rotation and the swimming speed in the absence of the methylation machinery each occurs in a small fraction of cells. Furthermore, deletion of the main enzyme responsible for acetylation of the signaling molecule CheY prevented speed adaptation but not adaptation of the direction of rotation. These results suggest that methylation-independent adaptation in bacterial chemotaxis involves chemokinetic adaptation, which is dependent on CheY acetylation.

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Acetylation of the Chemotaxis Response Regulator CheY by Acetyl-CoA Synthetase Purified from Escherichia coli

Cited by 61 publications

References 94 publications

The Acetate Switch

The Acetate Switch

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Methylation‐independent adaptation in chemotaxis of Escherichia coli involves acetylation‐dependent speed adaptation

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