Modulation of CRP‐dependent transcription at the <i>Escherichia coli acs</i>P2 promoter by nucleoprotein complexes: anti‐activation by the nucleoid proteins FIS and IHF

Browning, Douglas F.; Beatty, Christine M.; Sanstad, Erik A.; Gunn, Kathryn; Busby, Stephen J. W.; Wolfe, Alan J.

doi:10.1046/j.1365-2958.2003.03824.x

Cited by 57 publications

(53 citation statements)

References 34 publications

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“…Expression of acs is controlled by several transcription factors, including the nucleoid proteins Fis and integration host factor (IHF) as well as Crp (177,248). Interestingly, the E. coli protein acetyltransferase gene pka has an expression profile similar to that of its target, acs, during growth on glucose (177).…”

Section: Regulation Of Rla Genes In Escherichia Colimentioning

confidence: 99%

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

169

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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Section: Regulation Of Rla Genes In Escherichia Colimentioning

confidence: 99%

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

169

175

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“…As the Acs level increases, exogenous acetate is recaptured by Acs and Ack/Pta and is catabolized via the TCA cycle and glyoxylate bypass, increasing the amount of carbon and energy available for growth. Elegant studies of acs expression indicate that the Acs level is very low in lowdensity cultures (Browning et al, 2004), a fact that would explain the kinetics of acetate accumulation and recapture from the environment. The very efficient EutD phosphotransacetylase, in conjunction with acetate kinase, regenerates free CoA, a process that appears to also involve an as-yet-unidentified acetate-releasing system.…”

Section: Acetate Excretion During Growth On Ethanolamine Requires Eutmentioning

confidence: 99%

Acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities

2005

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This report shows that Salmonella enterica catabolizes ethanolamine to acetyl-CoA (Ac-CoA), which enters the glyoxylate bypass and tricarboxylic acid cycle for the generation of energy and central metabolites. During growth on ethanolamine, S. enterica excreted acetate, whose recapture depended on Ac-CoA synthetase (Acs) and the housekeeping phosphotransacetylase (Pta) enzyme activities. The Pta enzyme did not play a role in acetate excretion during growth of S. enterica on ethanolamine. It is proposed that during growth on ethanolamine, acetate excretion is necessary to maintain a pool of free CoA. Acetate excretion requires the eut operon-encoded phosphotransacetylase (EutD) and acetate kinase (Ack) enzymes. EutD function was not required for growth on ethanolamine, and an eutD strain showed only a slight reduction in growth rate. The existence of an as-yet-unidentified system that releases acetate was revealed during growth of a strain lacking Acs, the housekeeping phosphotransacetylase (Pta), and EutD. The functions of pyruvate oxidase (PoxB), Ack and STM3118 protein [a homologue of the Saccharomyces cerevisiae Ac-CoA hydrolase (Ach1p) enzyme] were not involved in the release of acetate by the acs pta eutD strain.

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“…Although some aspects of regulation by multiple global regulators have been studied (e.g. Browning et al, 2004;Germer et al, 2001;Johansson et al, 1998;Schneider et al, 2003;Soutourina et al, 1999), our current understanding of the complex mechanism of transcriptional reprogramming at the transition state is incomplete.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of a second, inducible promoter of relA in Escherichia coli

2006

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The alarmone ppGpp is an important signal molecule for the stringent response. Escherichia coli relA encodes a ppGpp synthetase, and although the regulation of RelA protein activity has been studied extensively, the regulation of relA transcription remains unclear. Here, we describe a novel relA promoter, relA P2. According to quantitative measurement of mRNA by primer extension analysis, the previously reported promoter relA P1 is constitutively active throughout growth, while relA P2 is induced temporarily at the transition state between the exponential growth and stationary phases. A chromosomal transcriptional lacZ fusion ( relA P2-lacZ ) showed that relA P2 is positively regulated by H-NS and CRP. Furthermore, the reduced activity of relA P2-lacZ in an hns mutant could be rescued by an rpoS mutation, which is sufficient to derepress the relA P2-lacZ activity. These data suggest that transient expression from the relA P2 promoter is controlled by several global regulators. This may account for the complex regulation of relA expression in Escherichia coli .

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Modulation of CRP‐dependent transcription at the Escherichia coli acsP2 promoter by nucleoprotein complexes: anti‐activation by the nucleoid proteins FIS and IHF

Cited by 57 publications

References 34 publications

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

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

Acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities

Identification and characterization of a second, inducible promoter of relA in Escherichia coli

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