Partial purification of the protein system controlling the breakdown of trehalose in baker's yeast

Solingen, P. van; Plaat, J.B. van der

doi:10.1016/0006-291x(75)90434-9

Cited by 76 publications

(53 citation statements)

References 12 publications

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“…By the uptake of Ta into the vacuoles trehalose mobilization in the cytosol may then eventually be terminated. In this context it is interesting that after a phase of trehalase induction in yeast the trehalase activity always decreases again quite rapidly [1,3,4]. Possibly Ta is unstable in the vacuoles as these are the lysosomes of yeast [6].…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Does a cyclic AMP‐dependent phosphorylation initiate the transfer of trehalase from the cytosol into the vacuoles in Saccharomyces cerevisiae?

Wiemken¹,

Schellenberg²

1982

FEBS Letters

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Trehalase activity in a yeast protoplast lysate increased ∼40‐times upon preincubation with cAMP and ATP. The activity present without the preincubation could all be sedimentated at 8000 × g, for 10 min confirming the previously reported localization of the active trehalase (Ta) in the vacuoles. Virtually all the trehalase activity newly formed upon the preincubation, however, was found in the soluble fraction, indicating that a trehelase‐zymogen (Tz) is located in the cytosol. This raises the possibility that a cAMP‐dependent phosphorylation not only transforms Tz to Ta but also initiates the transfer of trehalase from the cytosol into the vacuoles.

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Section: Discussionmentioning

confidence: 99%

“…This appears to involve activation of a preexisting trehalase-zymogen (Tz) by a cAMP-dependent protein kinase [3]. Having shown that the active trehalase (Ta) is located in the vacuoles [4] it interested us to see where the zymogen (Tz) is located.…”

Section: Introductionmentioning

confidence: 99%

Does a cyclic AMP‐dependent phosphorylation initiate the transfer of trehalase from the cytosol into the vacuoles in Saccharomyces cerevisiae?

Wiemken¹,

Schellenberg²

1982

FEBS Letters

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“…Protoplasts were obtained by a modification of the procedure of VAN SoLINGEN and VAN DER PLAAT (11). Cells from an approximately 18-24 hr culture (40 ml) in YM (C. maltosa) or YPD (S. cerevisiae) were collected by centrifugation, suspended in 5 ml of pretreatment solution containing 60 mM EDTA, 0.2 M 2-mercaptoethanol, 50 mM phosphate buffer (pH 7.5) and 1.2 M sorbitol, and incubated for 15 min at 30°.…”

Section: Methodsmentioning

confidence: 99%

Ploidy in the asporogenous yeast Candida maltosa, isolation of its auxotrophic mutants and their cell fusion.

Chang

Jung

Suzuki

et al. 1984

J. Gen. Appl. Microbiol.

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“…Neutral trehalase (EC 3.2.1.28), encoded by the NTH1 gene, has been reported to be post-translationally regulated by two main mechanisms: i) phosphorylation by cAMPdependent protein kinase (PKA) that converts the non-phosphorylated cryptic trehalase into the phosphorylated active form (1)(2)(3), and ii) down-regulation of the phosphorylation step by an unidentified protein (4).…”

Section: Introductionmentioning

confidence: 99%

Evidence for a modulation of neutral trehalase activity by Ca2+ and cAMP signaling pathways in Saccharomyces cerevisiae

Souza

Mesquita

Panek

et al. 2002

Braz J Med Biol Res

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Saccharomyces cerevisiae neutral trehalase (encoded by NTH1) is regulated by cAMP-dependent protein kinase (PKA) and by an endogenous modulator protein. A yeast strain with knockouts of CMK1 and CMK2 genes (cmk1cmk2) and its isogenic control (CMK1CMK2) were used to investigate the role of CaM kinase II in the in vitro activation of neutral trehalase during growth on glucose. In the exponential growth phase, cmk1cmk2 cells exhibited basal trehalase activity and an activation ratio by PKA very similar to that found in CMK1CMK2 cells. At diauxie, even though both cells presented comparable basal trehalase activities, cmk1cmk2 cells showed reduced activation by PKA and lower total trehalase activity when compared to CMK1CMK2 cells. To determine if CaM kinase II regulates NTH1 expression or is involved in post-translational modulation of neutral trehalase activity, NTH1 promoter activity was evaluated using an NTH1-lacZ reporter gene. Similar ß-galactosidase activities were found for CMK1CMK2 and cmk1cmk2 cells, ruling out the role of CaM kinase II in NTH1 expression. Thus, CaM kinase II should act in concert with PKA on the activation of the cryptic form of neutral trehalase. A model for trehalase regulation by CaM kinase II is proposed whereby the target protein for Ca 2+ /CaM-dependent kinase II phosphorylation is not the neutral trehalase itself. The possible identity of this target protein with the recently identified trehalaseassociated protein YLR270Wp is discussed.

show abstract

Partial purification of the protein system controlling the breakdown of trehalose in baker's yeast

Cited by 76 publications

References 12 publications

Does a cyclic AMP‐dependent phosphorylation initiate the transfer of trehalase from the cytosol into the vacuoles in Saccharomyces cerevisiae?

Does a cyclic AMP‐dependent phosphorylation initiate the transfer of trehalase from the cytosol into the vacuoles in Saccharomyces cerevisiae?

Ploidy in the asporogenous yeast Candida maltosa, isolation of its auxotrophic mutants and their cell fusion.

Evidence for a modulation of neutral trehalase activity by Ca2+ and cAMP signaling pathways in Saccharomyces cerevisiae

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