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  • 1
    Electronic Resource
    Electronic Resource
    Heat-shock response in Schizosaccharomyces pombe cells lacking cyclic AMP-dependent phosphorylation (1997)
    Springer
    Current genetics 31 (1997), S. 112-118 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsSchizosaccharomyces pombe ; Thermal resistance ; Cyclic AMP ; Trehalose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Heat sensitivity at 48°C was determined in log-phase cultures of control and pka1-disrupted cells of the fission yeast Schizosaccharomyces pombe grown at 25°C. Cells devoid of protein kinase A exhibited a considerable heat-shock resistance as compared to control cells. Addition of cAMP to control cells prompted a further decrease in viability during heat shock. This effect was not observed with pka1-disrupted cells, suggesting that cAMP-dependent phosphorylation is involved in modulation of the heat-shock response. When control or pka1-disrupted cells were grown at 25°C and then shifted to 37°C they acquired thermo-tolerance to a subsequent treatment at 48°C both in the absence and in the presence of exogenous cAMP. Inhibition of protein synthesis during the adaptive treatment did not block the development of thermo-tolerance. However, the arrest in translation significantly prevented trehalose accumulation in control cells but only slightly affected trehalose increase in pka1-disrupted cells. These data indicate that heat resistance may be established in growing cells of S. pombe by at least two independent post-translational mechanisms: a decrease in cAMP-dependent protein phosphorylation and a hitherto unknown process which may be independent of trehalose accumulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050183
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  • 2
    Electronic Resource
    Electronic Resource
    Proteolytic activation of α,α-trehalose 6-phosphate synthase in Candida utilis (1991)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 82 (1991), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: Total trehalose 6-phosphate synthase activity increased in cell-free extracts from Candida utilis following short-term preincubation of the enzyme samples at 37°C. This endogenous activation was prevented by the inhibitors of serine-type proteases, phenylmethylsulfonyl fluoride, antipain or chymostatin, but not by other protease inhibitors such as pepstatin. Fractionation of the cell extracts by Sephadex G-200 gel filtration revealed that the activity of one of the two synthase enzymes present in these cells was enhanced after the activation treatment. These observations indicate the existence of a proteolytically activatable enzyme form in the trehalose 6-phosphate synthase complex of this yeast in addition to the previously characterized enzyme, whose activity appears to be inactivated by reversible phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04858.x
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  • 3
    Electronic Resource
    Electronic Resource
    Presence of two trehalose-6-phosphate synthase enzymes in Candida utilis (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 61 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Total trehalose-6-phosphate synthase activity decreased in cell extracts from Candida utilis under conditions inducing activation of the regulatory trehalase by protein kinase catalysed phosphorylation. The synthase activity was reactivated by treatment with alkaline phosphatase revealing the presence of an enzyme whose activity is inactivated by reversible phosphorylation. The occurrence in the trehalose-6-phosphate synthase complex of a second synthase enzyme whose activity is not controlled by phosphorylation and dephosphorylation was demonstrated following gel filtration of cell extracts. The activity of the isolated enzymes was differently modified in vitro by the presence of alkaline phosphatase, ATP, glucose or protein kinase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03636.x
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  • 4
    Electronic Resource
    Electronic Resource
    Nitrogen-source-induced activation of neutral trehalase in Schizosaccharomyces pombe and Pachysolen tannophilus: role of cAMP as second messenger (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 132 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Resting cells of the fission yeast Schizosaccharomyces pombe, suspended in buffer with glucose, responded to the addition of asparagine by increasing trehalase activity. This response was preceded by a peak in cAMP concentration. The addition of the nitrogen source to resting cells, devoid of the catalytic subunit of cAMP-dependent protein kinase, produced the transient increase in cAMP but did not promote any change in trehalase activity. In the budding yeast Pachysolen iannophilus, the activation of trehalase by nitrogen source was also accompanied by a sharp peak in cAMP. These results suggest that in the two yeasts cAMP acts as a second messenger in the transduction of the nitrogen-source-induced signal causing the activation of trehalase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07838.x
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  • 5
    Electronic Resource
    Electronic Resource
    Role for trehalase during germination of spores in the fission yeast Schizosaccharomyces pombe (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 193 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Spores from Schizosaccharomyces pombe contain neutral and acid trehalases. When spores from strains disrupted for ntp1+, which encodes neutral trehalase, were induced to germinate, the onset of the process was markedly delayed as compared to wild-type spores. Further outgrowth was also reduced. Dormant spores lacking neutral trehalase contained twice the amount of trehalose present in wild-type spores and mobilised the intracellular pool of trehalose at a slower rate during germination. Inhibition by phloridzin of the sporulation-specific acid trehalase in ntp1-disrupted spores arrested germination completely while prompting no effect on wild-type spores. These results suggest that the two trehalase enzymes may support the utilisation of trehalose during germination but neutral trehalase is required for a more rapid and efficient process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb09412.x
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  • 6
    Electronic Resource
    Electronic Resource
    Protein phosphorylation and trehalase activation in Candida utilis (1986)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 34 (1986), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Candida utilis cells contain a regulatory trehalase enzyme (280 kDa) which can be activated by cAMP-dependent phosphorylation. A 100-fold purification of this enzyme activity results in the enrichment of a protein band of apparent Mr 70 000 as identified by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). This component is phosphorylated in vivo under conditions in which trehalase activation occurs in whole cells. It is concluded that the trehalase enzyme might be a tetramer, composed of 4 identical 70-kDa subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01437.x
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