Initiation of meiosis in yeast mutants defective in adenylate cyclase and cyclic AMP-dependent protein kinase

Matsumoto, Kunihiro; Uno, Isao; Ishikawa, Tatsuo

doi:10.1016/0092-8674(83)90461-0

Cited by 184 publications

(110 citation statements)

References 16 publications

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“…To find how these nutritional signals regulate entry into meiosis, transcript levels from meiotic inducer genes (I MEl and IME2) were examined under various culture conditions. Our results suggest (1) that IMEl RNA levels are negatively regulated by cell division or induced by cell division arrest at Gl phase, (2) that the Gl arrest is not sufficient to induce IME2 transcription, and (3) that IMEl and IME2 transcriptions are inhibited by either nitrogen or glucose. Acetate was required for full expressions of IMEl and IME2 RNAs, and this induction required de novo protein synthesis.…”

mentioning

confidence: 87%

Nutritional Regulation of Meiosis-specific Gene Expression in Saccharomyces cerevisiae

Kawaguchi

Yoshida

Yamashita

1992

Bioscience, Biotechnology, and Biochemistry

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mentioning

confidence: 87%

Nutritional Regulation of Meiosis-specific Gene Expression in Saccharomyces cerevisiae

Kawaguchi

Yoshida

Yamashita

1992

Bioscience, Biotechnology, and Biochemistry

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“…It is generally believed that the intracellular glucose phosphorylation signal is further transduced to the cAMP-PKA pathway via the Ras proteins, Ras1 and Ras2, which belong to the group of small G proteins. The GTPbound, active Ras proteins stimulate the activity of the adenylate cyclase Cyr1 (also known as Cdc35), the enzyme which catalyses the synthesis of cAMP from ATP (Casperson et al 1983(Casperson et al , 1985Matsumoto et al 1983Matsumoto et al , 1984Kataoka et al 1985;Toda et al 1985;Field et al 1988). The GDP/GTP exchange on the Ras proteins is controlled by the guanine nucleotide exchange factors (GEF) Cdc25 and Sdc25 (Broek et al 1987;Camonis and Jacquet 1988;Jones et al 1991;Camus et al 1994).…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

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Cells of all living organisms contain complex signal transduction networks to ensure that a wide range of physiological properties are properly adapted to the environmental conditions. The fundamental concepts and individual building blocks of these signalling networks are generally well-conserved from yeast to man; yet, the central role that growth factors and hormones play in the regulation of signalling cascades in higher eukaryotes is executed by nutrients in yeast. Several nutrient-controlled pathways, which regulate cell growth and proliferation, metabolism and stress resistance, have been defined in yeast. These pathways are integrated into a signalling network, which ensures that yeast cells enter a quiescent, resting phase (G 0 ) to survive periods of nutrient scarceness and that they rapidly resume growth and cell proliferation when nutrient conditions become favourable again. A series of well-conserved nutrient-sensory protein kinases perform key roles in this signalling network: i.e. Snf1, PKA, Tor1 and Tor2, Sch9 and Pho85-Pho80. In this review, we provide a comprehensive overview on the current understanding of the signalling processes mediated via these kinases with a particular focus on how these individual pathways converge to signalling networks that ultimately ensure the dynamic translation of extracellular nutrient signals into appropriate physiological responses.

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“…A possible role for cAMP in yeast could be to control cell proliferation [40] and the initiation of meiosis which precedes sporulation [41].…”

Section: Discussionmentioning

confidence: 99%

Catabolite repression in yeasts is not associated with low levels of cAMP

Eraso

Gancedo

1984

European Journal of Biochemistry

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The relationship between levels of CAMP and catabolite repression in yeasts has been investigated. Strains of Succharomyces cerevisiae, Schizosaccharomyces pomhe and Kluyuerornyces jrugilis were used. The yeasts were grown on different carbon sources to attain various degrees of repression. Galactose repressed as much as glucose, while maltose was less effective. Full derepression was achieved with ethanol.The enzymes tested were fructose-bisphosphatase, malate dehydrogenase, glutamate dehydrogenase (NAD dependent), cytochrome oxidase and isocitrate lyase (this last enzyme was found to be absent in Schizosaccharomyces).The levels of CAMP were 2 -3 times higher in the repressed conditions than in the derepressed ones. It is therefore concluded that in yeasts catabolite repression is not mediated by a lowering of the intracellular concentration of CAMP.Catabolite repression in yeasts is a well known phenomenon [I] but its underlying mechanism has not been yet established. Since in bacteria catabolite repression is correlated with lowered levels of CAMP (for a review see [2]), it has been tempting to assume that the same situation ocurred in yeast. Indeed some early data on CAMP levels appeared to confirm this idea [3,4] and a more recent review on the subject agreed also with this view [5]. However several results casted doubts on the role of CAMP in mediating catabolite repression in yeast. Montenecourt et al. [6] did not found a clear correlation between the cAMP level and the sensitivity of invertase synthesis to catabolite repression. Also, in yeast strains permeable to cAMP [7] the addition of exogenous cAMP did not prevent glucose repression of galactokinase synthesis [8]. Finally, it has been repeatedly shown that the addition of glucose to a Saccharomyces cerevisiae culture produces an increase in the levels of CAMP [9 -1 I], although this increase was thought to be transient.We decided therefore to reinvestigate systematically the relationship between CAMP levels and catabolite repression in yeasts. Our results show that in different yeast genera catabolite repression is not associated with a decreased level of CAMP. On the contrary, the lowest levels of CAMP are found in yeast not subject to catabolite repression. MATERIALS A N D METHODS Strains ojyeust and growth conditionsThe following yeast strains were used : Succharomyces cerevisiae F11 (obtained from G. Fink) and X2180, Sclzizosuccharomyces pomhe NCYC 972h-and Kluyverornyces fruEnzymes. Fructose-bisphosphatase (EC 3.1.3.11) ; isocitrate lyase (EC 4.1.3.1); malate dehydrogenase (EC 1.1.1.37); glutamate dehydrogenase (NAD dependent) (EC 1.4.1.2); cytochrome oxidase (EC 1.9.3.1).gilis 1407 (obtained from C. Gancedo). The yeasts were grown either on a complex medium with 1 % yeast extract and 2 % peptone or on a mineral medium [12] using NaCl (0.25 g/l) instead of the original sodium citrate and adjusting the initial pH of the medium to 5.5. The different carbon sources were added at 2 % final concentration unless otherwise indicated. Sampling of yeast...

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Initiation of meiosis in yeast mutants defective in adenylate cyclase and cyclic AMP-dependent protein kinase

Cited by 184 publications

References 16 publications

Nutritional Regulation of Meiosis-specific Gene Expression in Saccharomyces cerevisiae

Nutritional Regulation of Meiosis-specific Gene Expression in Saccharomyces cerevisiae

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

Catabolite repression in yeasts is not associated with low levels of cAMP

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