Extrusion of benzoic acid in 
               Saccharomyces cerevisiae
             by an energy-dependent mechanism

Henriques, Marília; Quintas, Célia; Loureiro-Dias, Maria C.

doi:10.1099/00221287-143-6-1877

Cited by 56 publications

(43 citation statements)

References 22 publications

(32 reference statements)

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“…Alteration of the plasma membrane composition upon sorbic acid stress in Z. rouxii was described previously (29). In addition, S. cerevisiae and Z. bailii cells adapted to benzoic acid have a reduced permeability to benzoate (33,71). We suggest that in B. subtilis, the observed induction of the fab genes and the bkd operon is a direct response to sorbic acid that will likely alter the membrane composition such that the diffusion rate of the organic molecule over the membrane is lowered.…”

Section: Discussionmentioning

confidence: 99%

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Transcriptome Analysis of Sorbic Acid-Stressed Bacillus subtilis Reveals a Nutrient Limitation Response and Indicates Plasma Membrane Remodeling

et al. 2008

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The weak organic acid sorbic acid is a commonly used food preservative, as it inhibits the growth of bacteria, yeasts, and molds. We have used genome-wide transcriptional profiling of Bacillus subtilis cells during mild sorbic acid stress to reveal the growth-inhibitory activity of this preservative and to identify potential resistance mechanisms. Our analysis demonstrated that sorbic acid-stressed cells induce responses normally seen upon nutrient limitation. This is indicated by the strong derepression of the CcpA, CodY, and Fur regulon and the induction of tricarboxylic acid cycle genes, SigL-and SigH-mediated genes, and the stringent response. Intriguingly, these conditions did not lead to the activation of sporulation, competence, or the general stress response. The fatty acid biosynthesis (fab) genes and BkdR-regulated genes are upregulated, which may indicate plasma membrane remodeling. This was further supported by the reduced sensitivity toward the fab inhibitor cerulenin upon sorbic acid stress. We are the first to present a comprehensive analysis of the transcriptional response of B. subtilis to sorbic acid stress.

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Section: Discussionmentioning

confidence: 99%

“…These processes, however, may reduce energy resources significantly (8,35,36). Studies with benzoic acid showed that adapted S. cerevisiae and Zygosaccharomyces bailii cells reduce their permeabilities to benzoate (33,71). Changes in fatty acid composition in sorbate-stressed Zygosaccharomyces rouxii cells have been reported (29).…”

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Transcriptome Analysis of Sorbic Acid-Stressed Bacillus subtilis Reveals a Nutrient Limitation Response and Indicates Plasma Membrane Remodeling

et al. 2008

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“…Nevertheless, Pdr12 action clearly enhances sorbate, benzoate and acetate resistance (Piper et al, 1998 ;Holyoak et al, 1999). Also it has long been known that acid-adapted S. cerevisiae and Z. bailii can maintain an intracellular versus extracellular distribution of benzoate that is not in equilibrium (Warth, 1977(Warth, , 1988(Warth, , 1989Henriques et al, 1997 ;Piper et al, 1998). This indicates the induction of a system whereby adapted cells can reduce their intracellular weak acid pool.…”

Section: What Is the Pdr12-inducing Signal?mentioning

confidence: 99%

Weak acid adaptation: the stress response that confers yeasts with resistance to organic acid food preservatives

et al. 2001

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“…Accumulation of radiolabeled acetic acid was determined essentially as described previously for measurements of the uptake of radiolabeled benzoic acid (10,23). Fifty-milliliter mid-exponential-phase cultures, grown at 30°C on pH 4.5 DO or YPD medium, were harvested and resuspended (5 ϫ 10 7 cells ml Ϫ1 ) in 6 ml of medium of the same pH containing 100 mM acetic acid, which was labeled with 25 Ci (15) (Amersham, United Kingdom).…”

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Hog1 Mitogen-Activated Protein Kinase Phosphorylation Targets the Yeast Fps1 Aquaglyceroporin for Endocytosis, Thereby Rendering Cells Resistant to Acetic Acid

Mollapour

Piper

2007

Molecular and Cellular Biology

242

251

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Aquaporins and aquaglyceroporins form the membrane channels that mediate fluxes of water and small solute molecules into and out of cells. Eukaryotes often use mitogen-activated protein kinase (MAPK) cascades for the intracellular signaling of stress. This study reveals an aquaglyceroporin being destabilized by direct MAPK phosphorylation and also a stress resistance being acquired through this channel loss. Hog1 MAPK is transiently activated in yeast exposed to high, toxic levels of acetic acid. This Hog1 then phosphorylates the plasma membrane aquaglyceroporin, Fps1, a phosphorylation that results in Fps1 becoming ubiquitinated and endocytosed and then degraded in the vacuole. As Fps1 is the membrane channel that facilitates passive diffusional flux of undissociated acetic acid into the cell, this loss downregulates such influx in low-pH cultures, where acetic acid (pK a , 4.75) is substantially undissociated. Consistent with this downregulation of the acid entry generating resistance, sensitivity to acetic acid is seen with diverse mutational defects that abolish endocytic removal of Fps1 from the plasma membrane (loss of Hog1, loss of the soluble domains of Fps1, a T231A S537A double mutation of Fps1 that prevents its in vivo phosphorylation, or mutations generating a general loss of endocytosis of cell surface proteins [doa4⌬ and end3⌬]). Remarkably, targetting of Fps1 for degradation may be the major requirement for an active Hog1 in acetic acid resistance, since Hog1 is largely dispensable for such resistance when the cells lack Fps1. Evidence is presented that in unstressed cells, Hog1 exists in physical association with the N-terminal cytosolic domain of Fps1.Baker's yeast (Saccharomyces cerevisiae) is extensively used as a model for studying how cells adapt to and survive different forms of stress. Its responses to hyperosmotic stress have been the subject of extensive investigations (11,12,21,26). Important for an adaptation to hyperosmotic conditions is counteracting the water loss from the cell, which is achieved in yeast by accumulating a high intracellular pool of glycerol. This glycerol acts as a compatible solute, ensuring that the proteins in the intracellular environment remain hydrated and protected. Osmostress adaptation also involves the activation of the highosmolarity glycerol (HOG) mitogen-activated protein kinase (MAPK) signaling cascades, which generate an activation of a multifunctional Hog1 MAPK. This activated Hog1 then translocates to the nucleus, where, by the phosphorylation of at least three separate transcription factors (Sko1, Hot1, and Smp1), it can generate an altered regulation of Ͼ10% of the total yeast genome (21). Active Hog1 has recently been found to exert important actions, much more instant than its effects on transcription, at the plasma membrane, where it directly phosphorylates certain of the membrane ion transporters in osmostressed cells in order to rapidly readjust the transmembrane fluxes of Na ϩ and K ϩ (26). In this work, we show that activated Hog1 can also...

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Extrusion of benzoic acid in Saccharomyces cerevisiae by an energy-dependent mechanism

Cited by 56 publications

References 22 publications

Transcriptome Analysis of Sorbic Acid-Stressed Bacillus subtilis Reveals a Nutrient Limitation Response and Indicates Plasma Membrane Remodeling

Transcriptome Analysis of Sorbic Acid-Stressed Bacillus subtilis Reveals a Nutrient Limitation Response and Indicates Plasma Membrane Remodeling

Weak acid adaptation: the stress response that confers yeasts with resistance to organic acid food preservatives

Hog1 Mitogen-Activated Protein Kinase Phosphorylation Targets the Yeast Fps1 Aquaglyceroporin for Endocytosis, Thereby Rendering Cells Resistant to Acetic Acid

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