Yeast fructose‐2,6‐bisphosphate 6‐phosphatase is encoded by PHO8, the gene for nonspecific repressible alkaline phosphatase

Plankert, Uwe; Purwin, Claudio; Holzer, Helmut

doi:10.1111/j.1432-1033.1991.tb15803.x

Cited by 28 publications

(21 citation statements)

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“…BAPTA, a tetravalent ion, may release these proteins from the membrane, and inhibit vacuole fusion, through its contribution to ionic strength. Vacuole fusion is commonly measured by an assay coupled to the activity of the zinc-metalloenzyme Pho8p, which is sensitive to divalent ion chelators (11). We now report that fusion assays with 5 mM Mg 2ϩ show little sensitivity to BAPTA when they are adjusted to a constant ionic strength and are performed in the presence of the heavy metal ion chelator TPEN (to obviate the effect of Zn 2ϩ chelation by BAPTA).…”

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confidence: 98%

Ion Regulation of Homotypic Vacuole Fusion in Saccharomyces cerevisiae

Starai¹,

Thorngren

Fratti³

et al. 2005

Journal of Biological Chemistry

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2؉ , ATP, and Sec18p for fusion is bypassed through the addition of Vam7p, vacuole fusion does not require any appreciable free divalent cations and can even be stimulated by their chelators. The similarity of these findings to those with liposomes, and the higher ion specificity of the regulation of proteins, suggests a working model in which ion interactions with bilayer lipids permit Rab-and SNARE-dependent membrane fusion.

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confidence: 98%

Ion Regulation of Homotypic Vacuole Fusion in Saccharomyces cerevisiae

Starai¹,

Thorngren

Fratti³

et al. 2005

Journal of Biological Chemistry

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“…rALPase (optimum pH 8) encoded by PHO8, which is also a glycoprotein, is located in the vacuole (Clark et al, 1982) and cleaves diverse substrates to retrieve phosphate from intracellular products. It was suggested that the most important substrate of Pho8p is fructose-2, 6-bisphosphate (Plankert et al, 1991).…”

Section: The Genes and Proteins Concerning Phosphorous Metabolismmentioning

confidence: 99%

The phosphatase system in Saccharomyces cerevisiae.

1997

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The yeast Saccharomyces cerevisiae has at least six species of acid and alkaline phosphatases with different cellular localizations, as well as inorganic phosphate (P i ) transporters. Most of the genes encoding these enzymes are coordinately repressed and derepressed depending on the P i concentration in the growth medium. The P i signals are conveyed to these genes through a regulatory circuit consisting of a set of positive and negative regulatory proteins. This phosphatase system is interested as one of the best systems for studying gene regulation in S. cerevisiae due to the simplicity of phenotype determination in genetic analysis. With this methodological advantage, considerable amounts of genetic and molecular evidence in phosphatase regulation have been accumulated in the past twenty-five years. This article summarizes the current progress of research into this subject.

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“…In S. cerevisiae, it is thought that polyP synthesis requires energy generated from glycolysis because polyP accumulation was affected by sugar concentration in the medium (Werner et al, 2005). It was also reported that fructose-2,6-bisphosphate 6-phosphatase, which controls glycolysis, was encoded by the PHO8 gene (Plankert et al, 1991). Thus, the possibility remains that Pho8p links polyP metabolism with glycolysis.…”

Section: Discussionmentioning

confidence: 99%

“…It was reported that ALP, encoded by a PHO8 gene, had substrate specificity for sugar phosphates, such as glucose-6-phosphate, fructose-2,6-bisphosphate, fructose 1,6-diphosphate (Plankert et al, 1991;Toh-e et al, 1976), phosphoprotein, and phosphopeptide (Donella-Deana et al, 1993). In S. cerevisiae, it is thought that polyP synthesis requires energy generated from glycolysis because polyP accumulation was affected by sugar concentration in the medium (Werner et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

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PHO8 gene coding alkaline phosphatase of Saccharomyces cerevisiae is involved in polyphosphate metabolism

Kizawa

Aono

Ohtomo

2016

J. Gen. Appl. Microbiol.

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None of the authors of this manuscript has any financial or personal relationship with other people or organizations that could inappropriately influence their work.this study was to confirm the relationship between alkaline phosphatase (ALP) and polyP metabolism in Saccharomyces cerevisiae. Our previous study suggests that a correlation exists between the amount of polyP and detectable ALP activity in arbuscular mycorrhizal (AM) fungi (Funamoto et al., 2007), which are obligate symbiotic microorganisms belonging to Glomeromycota (Schüßler et al., 2001) and which form associations with plant roots in a host nonspecific manner.AM fungi absorb Pi from the soil via extraradical hyphae. Absorbed Pi is then converted to polyP and translocates to arbuscules formed in the cortical cells of the plant root (Smith and Read, 1996). Enzymatic-histochemical experiments showed that ALP activity were detected in arbuscules (Ezawa et al., 1995;Gianinazzi et al., 1979;Tisserant et al., 1993). Additionally, it has been speculated that hydrolyzation of polyP occurs in arbuscules. ALP has occasionally been considered to be involved in polyP metabolism. However, analysis using the ALP specific inhibitor, Be 2+ , suggests that ALP of AM fungi has a high substrate specificity for sugar-phosphates, such as glucose-6-Pi and trehalose-6-Pi (Ezawa et al., 1999). Previously, our studies have demonstrated that ALP activity was high in arbuscules and polyP accumulation was low (Funamoto et al., 2007). Furthermore, when the expression of the AM-inducible Pi transporter gene of host plants was suppressed, the expression of AM ALP gene (GiALP) (Aono et al., 2004), which bears a high similarity to the Pi-deficient-induced type ALP gene (PHO8) of S. cerevisiae, was suppressed, and the ALP activity decreased and polyP accumulated in mature arbuscules (Funamoto et al., 2007). These results point to the hypothesis that ALP may play some role in polyP metabolism in arbuscules. However, it is difficult to obtain direct evidence to verify this hypothesis because conventional molecular biology methods, such as transformation and gene disruption, cannot be used in the case of AM fungi.

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Yeast fructose‐2,6‐bisphosphate 6‐phosphatase is encoded by PHO8, the gene for nonspecific repressible alkaline phosphatase

Cited by 28 publications

References 20 publications

Ion Regulation of Homotypic Vacuole Fusion in Saccharomyces cerevisiae

Ion Regulation of Homotypic Vacuole Fusion in Saccharomyces cerevisiae

The phosphatase system in Saccharomyces cerevisiae.

<i>PHO8</i> gene coding alkaline phosphatase of <i>Saccharomyces cerevisiae</i> is involved in polyphosphate metabolism

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