Action of arsenate in glycolysis

Pillai, Raman Kochukrishna

doi:10.1042/bj0321961

Cited by 6 publications

(2 citation statements)

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“…Arsenate exerts its toxicity as a phosphate analog, where it substitutes for Pi in phosphorylation reactions. Since the arsenylated products are unstable, As(V) uncouples substrate‐level phosphorylation reactions in glycolysis (Pillai, ) and ATP production in oxidative phosphorylation (Azzone and Ernster, ). Yet nearly every microbial protein involved in resistance to arsenicals uses the trivalent species as a ligand or substrate, including the As(III)‐responsive transcriptional repressor ArsR (Shi et al ., ), the As(III) metallochaperone ArsD (Lin et al ., ), the ArsA As(III) ATPase (Rosen et al ., ), the ArsB and Acr3 As(III) efflux permeases (Meng et al ., ; Villadangos et al ., ), the ArsM As(III) S‐adenosylmethionine methyltransferase (Qin et al ., ).…”

Section: Discussionmentioning

confidence: 99%

Synergistic interaction of glyceraldehydes‐3‐phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance

Chen

Yoshinaga

Garbinski

et al. 2016

Molecular Microbiology

104

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Summary Microbial biotransformations are major contributors to the arsenic biogeocycle. In parallel with transformations of inorganic arsenic, organoarsenicals pathways have recently been recognized as important components of global cycling of arsenic. The well-characterized pathway of resistance to arsenate is reduction coupled to arsenite efflux. Here, we describe a new pathway of arsenate resistance involving biosynthesis and extrusion of an unusual pentavalent organoarsenical. A number of arsenic resistance (ars) operons have two genes of unknown function that are linked in these operons. One, gapdh, encodes the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. The other, arsJ, encodes a major facilitator superfamily (MFS) protein. The two genes were cloned from the chromosome of Pseudomonas aeruginosa. When expressed together, but not alone, in Escherichia coli, gapdh and arsJ specifically conferred resistance to arsenate and decreased accumulation of As(V). Everted membrane vesicles from cells expressing arsJ accumulated As(V) in the presence of purified GAPDH, D-glceraldehylde 3-phosphate (G3P) and NAD+. GAPDH forms the unstable organoarsenical 1-arseno-3-phosphoglycerate (1As3PGA). We propose that ArsJ is an efflux permease that extrudes 1As3PGA from cells, where it rapidly dissociates into As(V) and 3-phosphoglycerate (3PGA), creating a novel pathway of arsenate resistance.

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Section: Discussionmentioning

confidence: 99%

Synergistic interaction of glyceraldehydes‐3‐phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance

Chen

Yoshinaga

Garbinski

et al. 2016

Molecular Microbiology

104

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“…However, when treated with the inhibitor under anaerobic conditions, neither strain was able to express an SSR. Sodium arsenate, though not specific in its mode of action, has been shown to deplete intracellular ATP (Pillai, 1938). The depletion of intracellular ATP upon sodium arsenate addition coupled with less ATP production through anaerobic fermentation possibly explains why L. monocytogenes cells kept anaerobically appeared to be more adversely affected than those incubated aerobically.…”

Section: Effect Of Inhibitors Of Oxidative Phosphorylation On the Ssrmentioning

confidence: 92%

The Combination of Energy-Dependent Internal Adaptation Mechanisms and External Factors EnablesListeria monocytogenesto Express a Strong Starvation Survival Response During Multiple-Nutrient Starvation

Lungu

Saldivar

Story

et al. 2010

Foodborne Pathogens and Disease

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The goal of this study was to characterize the starvation survival response (SSR) of a wild-type Listeria monocytogenes 10403S and an isogenic DeltasigB mutant strain during multiple-nutrient starvation conditions over 28 days. This study examined the effects of inhibitors of protein synthesis, the proton motive force, substrate level phosphorylation, and oxidative phosphorylation on the SSR of L. monocytogenes 10403S and a DeltasigB mutant during multiple-nutrient starvation. The effects of starvation buffer changes on viability were also examined. During multiple-nutrient starvation, both strains expressed a strong SSR, suggesting that L. monocytogenes possesses SigB-independent mechanism(s) for survival during multiple-nutrient starvation. Neither strain was able to express an SSR following starvation buffer changes, indicating that the nutrients/factors present in the starvation buffer could be a source of energy for cell maintenance and survival. Neither the wild-type nor the DeltasigB mutant strain was able to elicit an SSR when exposed to the protein synthesis inhibitor chloramphenicol within the first 4 h of starvation. However, both strains expressed an SSR when exposed to chloramphenicol after 6 h or more of starvation, suggesting that the majority of proteins required to elicit an effective SSR in L. monocytogenes are likely produced somewhere between 4 and 6 h of starvation. The varying SSRs of both strains to the different metabolic inhibitors under aerobic or anaerobic conditions suggested that (1) energy derived from the proton motive force is important for an effective SSR, (2) L. monocytogenes utilizes an anaerobic electron transport during multiple-nutrient starvation conditions, and (3) the glycolytic pathway is an important energy source during multiple-nutrient starvation when oxygen is available, and less important under anaerobic conditions. Collectively, the data suggest that the combination of energy-dependent internal adaptation mechanisms of cells and external nutrients/factors enables L. monocytogenes to express a strong SSR.

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Biological Oxidation-Reduction Catalysts

Elliott¹

1941

Biokatalyse

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Action of arsenate in glycolysis

Cited by 6 publications

References 4 publications

Synergistic interaction of glyceraldehydes‐3‐phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance

Synergistic interaction of glyceraldehydes‐3‐phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance

The Combination of Energy-Dependent Internal Adaptation Mechanisms and External Factors EnablesListeria monocytogenesto Express a Strong Starvation Survival Response During Multiple-Nutrient Starvation

Biological Oxidation-Reduction Catalysts

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