The role of an active transport mechanism in glycerol accumulation during osmoregulation by Zygosaccharomyces rouxii

Zyl, Petrus Jakobus van; Kilian, S. G.; Prior, Bernard A.

doi:10.1007/bf00166787

Cited by 65 publications

(28 citation statements)

References 16 publications

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“…Fusarium oxysporum (8) and E. coli (2) transport glycerol by facilitated diffusion, whereas active transport occurs in Z. rouxii, D. hansenii and P. sorbitophila (1,21,36). Since E. coli GlpF complements the loss of glycerol transport in the S. cerevisiae fps1⌬ mutant, a comparison between these two systems is of interest.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, specific transport proteins are frequently produced by microorganisms, resulting in more rapid transport of glycerol across the membrane. Active glycerol transport systems requiring the expenditure of metabolic energy have been identified in Zygosaccharomyces rouxii, Debaryomyces hansenii and Pichia sorbitophila (21,23,36), whereas glycerol crosses the Escherichia coli cytoplasmic membrane via a proteinaceous pore mechanism which is encoded by glpF (15).…”

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Characteristics of Fps1-dependent and -independent glycerol transport in Saccharomyces cerevisiae

et al. 1997

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Eadie-Hofstee plots of glycerol uptake in wild-type Saccharomyces cerevisiae W303-1A grown on glucose showed the presence of both saturable transport and simple diffusion, whereas an fps1⌬ mutant displayed only simple diffusion. Transformation of the fps1⌬ mutant with the glpF gene, which encodes glycerol transport in Escherichia coli, restored biphasic transport kinetics. Yeast extract-peptone-dextrose-grown wild-type cells had a higher passive diffusion constant than the fps1⌬ mutant, and ethanol enhanced the rate of proton diffusion to a greater extent in the wild type than in the fps1⌬ mutant. In addition, the lipid fraction of the fps1⌬ mutant contained a lower percentage of phospholipids and a higher percentage of glycolipids than that of the wild type. Fps1p, therefore, may be involved in the regulation of lipid metabolism in S. cerevisiae, affecting membrane permeability in addition to fulfilling its specific role in glycerol transport. Simultaneous uptake of glycerol and protons occurred in both glycerol-and ethanol-grown wild-type and fps1⌬ cells and resulted in the accumulation of glycerol at an inside-to-outside ratio of 12:1 to 15:1. Carbonyl cyanide m-chlorophenylhydrazone prevented glycerol accumulation in both strains and abolished transport in the fps1⌬ mutant grown on ethanol. Likewise, 2,4-dinitrophenol inhibited transport in glycerol-grown wild-type cells. These results indicate the presence of an Fps1p-dependent facilitated diffusion system in glucose-grown cells and an Fps1p-independent proton symport system in derepressed cells.Glycerol crosses all biological membranes by passive diffusion due to its lipophilic nature. In addition, specific transport proteins are frequently produced by microorganisms, resulting in more rapid transport of glycerol across the membrane. Active glycerol transport systems requiring the expenditure of metabolic energy have been identified in Zygosaccharomyces rouxii, Debaryomyces hansenii and Pichia sorbitophila (21,23,36), whereas glycerol crosses the Escherichia coli cytoplasmic membrane via a proteinaceous pore mechanism which is encoded by glpF (15).It has been assumed that glycerol is taken up by Saccharomyces cerevisiae by passive diffusion only. Recently FPS1, which encodes a protein belonging to the MIP family, has been shown to affect the movement of glycerol across the membrane of S. cerevisiae (24). The FPS1 gene was isolated as a multicopy suppressor of the growth defect on fermentable sugars of a yeast fdp1 (FDP1 is also known as CIF1 and GGS1) mutant (33). Fps1p seems to play an important role in glycerol efflux, since mutants lacking FPS1 fail to rapidly release excess glycerol when hyperosmotic stress is relieved and during glycerol overproduction (reference 24 and unpublished results).The MIP family is a group of channel proteins present in organisms ranging from bacteria to humans (28). Most of these proteins are around 250 to 280 amino acids long and consist of six membrane-spanning segments. Fps1p differs from most members of the MIP family b...

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Section: Discussionmentioning

confidence: 99%

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Characteristics of Fps1-dependent and -independent glycerol transport in Saccharomyces cerevisiae

et al. 1997

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“…Since the volume of the medium is much larger than that of the cells, uptake of external (54) and D. hansenii (1), but no evidence has been found yet for such a system in S. cerevisiae (9). Probably, a glycerol transport mechanism has escaped attention in wild-type cells because of a balance between uptake of glycerol and leakage of internally produced glycerol.…”

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confidence: 99%

“…In S. cerevisiae, glycerol seems to be the only compatible solute produced and there appear to be mechanisms to specifically retain the glycerol in the cell (2; for reviews, see references 9 and 33). However, this effect is much more pronounced in highly osmotolerant yeasts such as Zygosaccharomyces rouxii or Debaryomyces hansenii (1,54). Although the correlation between the growth of yeast cells under osmotic stress conditions and enhanced glycerol production has always been apparent, it has not yet been possible to assess the actual intermediate dihydroxyacetonephosphate in two steps that are catalyzed, respectively, by an NADH-dependent glycerol-3-phosphate dehydrogenase (GPDH) and a probably unspecific phosphatase (3).…”

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GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway.

Albertyn¹,

Hohmann²,

Thevelein³

et al. 1994

Mol. Cell. Biol.

605

600

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The yeast Saccharomyces cerevisiae responds to osmotic stress, i.e., an increase in osmolarity of the growth medium, by enhanced production and intracellular accumulation of glycerol as a compatible solute. We have cloned a gene encoding the key enzyme of glycerol synthesis, the NADH-dependent cytosolic glycerol-3-phosphate dehydrogenase, and we named it GPD1. gpdlA mutants produced very little glycerol, and they were sensitive to osmotic stress. Thus, glycerol production is indeed essential for the growth of yeast cells during reduced water availability. hoglA mutants lacking a protein kinase involved in osmostress-induced signal transduction (the high-osmolarity glycerol response [HOG] pathway) failed to increase glycerol-3-phosphate dehydrogenase activity and mRNA levels when osmotic stress was imposed. Thus, expression of GPD1 is regulated through the HOG pathway. However, there may be Hogl-independent mechanisms mediating osmostress-induced glycerol accumulation, since a hoglA strain could still enhance its glycerol content, although less than the wild type. hoglA mutants are more sensitive to osmotic stress than isogenic gpdlA strains, and gpdlA hoglA double mutants are even more sensitive than either single mutant. Thus, the HOG pathway most probably has additional targets in the mechanism of adaptation to hypertonic medium.

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“…Glycerol production has been widely studied by several microorganisms including Candida , Pichia (Hartlep et al, 2002) and Zygosacharomyces ( Van et al, 1990). Also, as bio-diesel is produced by the transesterification of plant seed oils, the glycerol is the main by-product.…”

Section: Introductionmentioning

confidence: 99%

Production of 1,3-propanediol by Klebsiella pneumoniae using raw glycerol from Zygosacharomyces rouxii

Ma¹,

Shentu²,

Bian³

et al. 2012

Afr. J. Biotechnol.

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The conversion of glycerol to 1,3-propanediol (1,3-PD) is an environmentally friendly biological process and has attracted great interests worldwide. Efficient utilization of raw glycerol could bring significant economic benefits for 1,3-PD production. In the present study, the glycerol broth from strain Zygosacharomyces rouxii JL2011 was first used as the sole carbon source for 1,3-PD production by Klebsiella pneumoniae. The result indicates that the glycerol broth affected K. pneumoniae growth and 1,3-PD yield dramatically. Therefore, the raw glycerol was further prepared by extraction and purification, and the effect of raw glycerol on 1,3-PD production was investigated. The results obtained showed that the purified glycerol could be directly utilized in shake-flask culture by K. pneumoniae with a result comparable with that attained from pure glycerol. In addition, the fed-batch culture using raw glycerol as the substrate was conducted giving 56.1 g⋅ ⋅ ⋅ ⋅L -1 with a yield of 0.40 g⋅ ⋅ ⋅ ⋅g -1 glycerol and productivity of 1.12 g⋅ ⋅ ⋅ ⋅L

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The role of an active transport mechanism in glycerol accumulation during osmoregulation by Zygosaccharomyces rouxii

Cited by 65 publications

References 16 publications

Characteristics of Fps1-dependent and -independent glycerol transport in Saccharomyces cerevisiae

Characteristics of Fps1-dependent and -independent glycerol transport in Saccharomyces cerevisiae

GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway.

Production of 1,3-propanediol by Klebsiella pneumoniae using raw glycerol from Zygosacharomyces rouxii

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