In silico and in vivo analysis reveal a novel gene in Saccharomyces cerevisiae trehalose metabolism

Mesquita, Joelma Freire De; Panek, Anita D.; Araujo, Pedro Soares De

doi:10.1186/1471-2164-4-45

Cited by 22 publications

(14 citation statements)

References 23 publications

(42 reference statements)

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“…A genome-wide yeast two-hybrid study had reported interaction between trehalase and YLR270w (49). Additional research by the Panek laboratory (28, 50) confirmed the role of Dcs1 as an inhibitor of trehalase activity. To gain more insight into the role of Dcs1 in trehalase regulation, we assessed nutrient-induced trehalase activation under a variety of conditions in a dcs1 Δ strain.…”

Section: Resultsmentioning

confidence: 90%

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In Vivo Phosphorylation of Ser21 and Ser83 during Nutrient-induced Activation of the Yeast Protein Kinase A (PKA) Target Trehalase

Schepers

Zeebroeck

Pinkse

et al. 2012

Journal of Biological Chemistry

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Background: Activation of yeast trehalase has been a convenient read-out for nutrient signaling to PKA, but demonstration of phosphorylation in vivo is lacking.Results: Nutrient activation is associated with phosphorylation, but phosphorylation is not enough for activation.Conclusion: Nutrient activation of trehalase is a reliable read-out for nutrient activation of PKA in vivo.Significance: Nutrient-sensing mechanisms can be identified using trehalase activation as a read-out.

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Section: Resultsmentioning

confidence: 90%

“…Two such mechanisms have been identified. Dcs1, an mRNA decapping enzyme, has been shown to interact with and act as a negative regulator of trehalase activity (28, 29). The yeast 14-3-3 proteins, encoded by Bmh1 and Bmh2, have recently been demonstrated to bind to phosphorylated residues in the N terminus of trehalase.…”

Section: Introductionmentioning

confidence: 99%

In Vivo Phosphorylation of Ser21 and Ser83 during Nutrient-induced Activation of the Yeast Protein Kinase A (PKA) Target Trehalase

Schepers

Zeebroeck

Pinkse

et al. 2012

Journal of Biological Chemistry

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“…Consistent with this hypothesis, we find that PKA inactivation leads to dramatically higher cAMP levels. PKA has also been shown to inhibit trehalose-6-phosphate phosphatase, whose product is trehalose, and to activate trehalase, which converts trehalose into glucose (Arguelles et al, 1993; De Mesquita et al, 2003; Francois et al, 1991). Such regulation would predict that inhibition of PKA should lead to accumulation of trehalose, as we observe.…”

Section: Resultsmentioning

confidence: 99%

Regulation of Yeast Pyruvate Kinase by Ultrasensitive Allostery Independent of Phosphorylation

Zhao

Glass

et al. 2012

Molecular Cell

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Summary Allostery and covalent modification are major means of fast-acting metabolic regulation. Their relative roles in responding to environmental changes remain, however, unclear. Here we examine this issue, using as a case study the rapid decrease in pyruvate kinase flux in yeast upon glucose removal. The main pyruvate kinase isozyme (Cdc19) is phosphorylated in response to environmental cues. It also exhibits positively-cooperative (ultrasensitive) allosteric activation by fructose-1,6-bisphosphate (FBP). Glucose removal causes accumulation of Cdc19’s substrate, phosphoenolpyruvate. This response is retained in strains with altered protein-kinase-A or AMP-activated-protein-kinase activity or with CDC19 carrying mutated phosphorylation sites. In contrast, yeast engineered with a CDC19 point mutation that ablates FBP-based regulation fail to accumulate phosphoenolpyruvate. They also fail to grow on ethanol and slowly resume growth upon glucose upshift. Thus, while yeast pyruvate kinase is covalently modified in response to glucose availability, its activity is controlled almost exclusively by ultrasensitive allostery.

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“…Furthermore, DCS2 , a gene homologous to the DCS1 ‐encoded decapping enzyme, shows 80% depletion in induction levels in the yap4 mutant. Recently, DCS1 has been described as an inhibitor of trehalase activity [57] that may have implications for osmo‐response due to the role of trehalose as a superior cellular osmolyte providing protection against dehydration and desiccation [58,59]. The complete identification of the remaining YAP4 target genes will greatly contribute towards the understanding of its functional role.…”

Section: Yap4p and Yap6p In The Response To Osmotic Stressmentioning

confidence: 99%

Yeast activator proteins and stress response: an overview

et al. 2004

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Yeast, and especially Saccharomyces cerevisiae, are continuously exposed to rapid and drastic changes in their external milieu. Therefore, cells must maintain their homeostasis, which is achieved through a highly coordinated gene expression involving a plethora of transcription factors, each of them performing specific functions. Here, we discuss recent advances in our understanding of the function of the yeast activator protein family of eight basic-leucine zipper trans-activators that have been implicated in various forms of stress response.

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In silico and in vivo analysis reveal a novel gene in Saccharomyces cerevisiae trehalose metabolism

Cited by 22 publications

References 23 publications

In Vivo Phosphorylation of Ser21 and Ser83 during Nutrient-induced Activation of the Yeast Protein Kinase A (PKA) Target Trehalase

In Vivo Phosphorylation of Ser21 and Ser83 during Nutrient-induced Activation of the Yeast Protein Kinase A (PKA) Target Trehalase

Regulation of Yeast Pyruvate Kinase by Ultrasensitive Allostery Independent of Phosphorylation

Yeast activator proteins and stress response: an overview

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