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Title: The Sch9 protein kinase in the yeast Saccharomyces cerevisiae controls cAPK activity and is required for nitrogen activation of the fermentable-growth-medium-induced (FGM) pathway
Authors: Crauwels, Marion
Donaton, MCV
Pernambuco, MB
Winderickx, Joris
deWinde, JH
Thevelein, Johan # ×
Issue Date: Aug-1997
Publisher: Soc general microbiology
Series Title: Microbiology vol:143 pages:2627-2637
Abstract: In cells of the yeast Saccharomyces cerevisiae, trehalase activation, repression of CTT1 (catalase), SSA3 (Hsp7O) and other STRE-controlled genes, feedback inhibition of cAMP synthesis and to some extent induction of ribosomal protein genes is controlled by the Ras-adenylate cyclase pathway and by the fermentable-growth-medium-induced pathway (FGM pathway). When derepressed cells are shifted from a non-fermentable carbon source to glucose, the Ras-adenylate cyclase pathway is transiently activated while the FCM pathway triggers a more lasting activation of the same targets when the cells become glucose-repressed. Activation of the FGM pathway is not mediated by cAMP but requires catalytic activity of cAMP-dependent protein kinase (cAPK; Tpk1, 2 or 3). This study shows that elimination of Sch9, a protein kinase with homology to the catalytic subunits of cAPK, affects ail target systems in derepressed cells in a way consistent with higher activity of cAPK in vivo. In vitro measurements with trehalase and kemptide as substrates confirmed that elimination of Sch9 enhances cAPK activity about two-to threefold, in both the absence and presence of cAMP. In vivo it similarly affected the basal and final level but not: the extent of the glucose-induced responses in derepressed cells. The reduction in growth rate caused by deletion of SCH9 is unlikely to be responsible for the increase in cAPK activity since reduction of growth rate generally leads to lower cAPK activity in yeast. On the other hand, deletion of SCH9 abolished the responses of the protein kinase A targets in glucose-repressed cells. Re-addition of nitrogen to cells starved for nitrogen in the presence of glucose failed to trigger activation of trehalase, caused strongly reduced and aberrant repression of CTT1 and SSA3, and failed to induce the upshift in RPL25 expression. From these results three conclusions can be drawn: (1) Sch9 either directly or indirectly reduces the activity of protein kinase A; (2) Sch9 is not required for glucose-induced activation of the Rasadenylate cyclase pathway; and (3) Sch9 is required for nitrogen-induced activation of the FCM pathway. The latter indicates that Sch9 might be the target of the FGM pathway rather than cAPK itself.
ISSN: 1350-0872
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Biology - miscellaneous
Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Molecular Microbiology and Biotechnology Section - miscellaneous
× corresponding author
# (joint) last author

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