Control of Saccharomyces cerevisiae Catalase T Gene (CTT1) Expression by Nutrient Supply via the RAS-Cyclic AMP Pathway

LITERATURE CITED

• Aviv, H., and Leder P.. 1972. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc. Natl. Acad. Sci. USA 69:1408–1412.
   PubMed Web of Science ®Google Scholar
• Boy-Marcotte, E., Gareau H., and Jacquet M.. 1987. Cyclic AMP controls the switch between division cycle and resting state programs in response to ammonium availability in Saccharomyces cerevisiae. Yeast 3:85–93.
   PubMedGoogle Scholar
• Bradford, M. M.. 1976. A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
   PubMed Web of Science ®Google Scholar
• Breeden, L., and Nasmyth K.. 1989. Regulation of the yeast HO gene. Cold Spring Harbor Symp. Quant. Biol. 50:643–650.
   Google Scholar
• Broach, J. R., Strathern J. N., and Hicks J.B.. 1979. Transformation in yeast: development of a hybrid cloning vector and isolation of the CAN I gene. Gene 8:121–133.
   PubMed Web of Science ®Google Scholar
• Broek, D., Toda T., Michaeli T., Levin L., Birchmeier C., Zoller M., Powers S., and Wigler M.. 1987. The S. cerevisiae CDC25 gene product regulates the /?AS/adenylate cyclase pathway. Cell 48:789–799.
   PubMed Web of Science ®Google Scholar
• Camonis, J. H., Kalekine M., Goudre B., Garreau H., Boy-Marcotte E., and Jacquet M.. 1986. Characterization, cloning and sequence analysis of the CDC25 gene which controls the cyclic AMP level of Saccharomyces cerevisiae. EMBO J. 5:375–380.
   PubMedGoogle Scholar
• Cannon, J. F., Gibbs J. B., and Tatchell K.. 1986. Suppressors of the ras2 mutation of Saccharomyces cerevisiae. Genetics 113:247–264.
   PubMedGoogle Scholar
• Cannon, J. F., and Tatchell K.. 1987. Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase. Mol. Cell. Biol. 7:2653–2663.
   PubMedGoogle Scholar
• Chvojka, A., Barlas M., Ruis H., Padrao G. R. C. B., Panek A. D., and Mattoon J. R.. 1981. A regulatory mutation in yeast which affects catalase T formation and metabolism of carbohydrate reserves. Curr. Genet. 4:47–50.
   PubMedGoogle Scholar
• Cohen, G., Fessl F., Traczyk A., Rytka J., and Ruis H.. 1989. Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the ctal mutation. Mol. Gen. Genet. 200: 74–79.
   Google Scholar
• Daniel, J., Becker J. M., Enari E., and Levitzki A.. 1987. The activation of adenylate cyclase by guanyl nucleotides in Saccharomyces cerevisiae is controlled by the CDC25 start gene product. Mol. Cell. Biol. 7:3857–3861.
   PubMedGoogle Scholar
• Esposito, R. E., and Klapholz S.. 1981. Meiosis and ascospore development, p. 211–287. In Strathern J., Jones E., and Broach J. (ed.), The molecular biology of the yeast Saccharomyces—life cycle and inheritance. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Feinberg, A. P., and Vogelstein B.. 1983. A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6–13.
   PubMed Web of Science ®Google Scholar
• Fink, G. R.. 1970. The biochemical genetics of yeast. Methods Enzymol. 17A:59–78.
   Google Scholar
• Hamilton, B., Hofbauer R., and Ruis H.. 1982. Translational control of catalase synthesis by hemin in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 79:7609–7613.
   PubMed Web of Science ®Google Scholar
• Hartig, A., and Ruis H.. 1986. Nucleotide sequence of the Saccharomyces cerevisiae CTT1 gene and deduced amino-acid sequence of yeast catalase T. Eur. J. Biochem. 160:487–490.
   PubMedGoogle Scholar
• Hortner, H., Ammerer G., Hartter E., Hamilton B., Rytka J., Bilinski T., and Ruis H.. 1982. Regulation of synthesis of catalases and iso-l-cytochrome c in Saccharomyces cerevisiae by glucose, oxygen and heme. Eur. J. Biochem. 128:179–184.
   PubMedGoogle Scholar
• Johnston, G. C, Pringle J. R., and Hart well L. H.. 1977. Coordination of growth with cell division in the yeast Saccharomyces cerevisiae. Exp. Cell Res. 105:79–98.
   PubMed Web of Science ®Google Scholar
• Kataoka, T., Powers S., McGill C., Fasano O., Strathern J., Broach J., and Wigler M.. 1984. Genetic analysis of yeast RAS1 and RAS2 genes. Cell 37:437–445.
   PubMed Web of Science ®Google Scholar
• Lillie, S. H., and Pringle J. R.. 1980. Reverse carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation. J. Bacterid. 143:1384–1394.
   PubMed Web of Science ®Google Scholar
• Matsumoto, K., Uno I., and Ishikawa T.. 1989. Genetic analysis of the role of cAMP in yeast. Yeast 1:15–24.
   Google Scholar
• Matsumoto, K., Uno I., Ishikawa T., and Oshima Y.. 1983. Cyclic AMP may not be involved in catabolite repression in Saccharomyces cerevisiae: evidence from mutants unable to synthesize it. J. Bacteriol. 156:898–900.
   PubMedGoogle Scholar
• Matsumoto, K., Uno I., Kato K., and Ishikawa T.. 1989. Isolation and characterization of a phosphoprotein phosphatase-deficient mutant in yeast. Yeast 1:25–38.
   Google Scholar
• Mendenhall, M. D., Jones C. A., and Reed S. I.. 1987. Dual regulation of the yeast CDC28-p40 protein kinase complex: cell cycle, pheromone, and nutrient limitation effects. Cell 50: 927–935.
   PubMedGoogle Scholar
• Miller, J. H.. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Pfeifer, K., Prezant T., and Guarente L.. 1987. Yeast HAP1 activator binds to two upstream activation sites of different sequence. Cell 49:19–27.
   PubMedGoogle Scholar
• Pringle, J. R., and Hart well L. H.. 1982. The Saccharomyces cerevisiae cell cycle, p. 97–142. In Strathern J., Jones E., and Broach J. (ed.), The molecular biology of the yeast Saccharomyces—life cycle and inheritance. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Rose, M., and Botstein D.. 1983. Construction and use of gene fusions to lacZ (β-galactosidase) that are expressed in yeast. Methods Enzymol. 101:167–180.
   PubMed Web of Science ®Google Scholar
• Rothman-Denes, L. B., and Cabib E.. 1970. Two forms of yeast glycogen synthetase and their role in glycogen accumulation. Proc. Natl. Acad. Sci. USA 66:967–974.
   PubMedGoogle Scholar
• Ruis, H.. 1979. The biosynthesis of catalase. Can. J. Biochem. 57:1122–1130.
   PubMedGoogle Scholar
• Seah, T. C. M., Bhatti A. R., and Kaplan J. G.. 1973. Novel catalatic proteins of bakers' yeast. I. An atypical catalase. Can. J. Biochem. 51:1551–1555.
   PubMedGoogle Scholar
• Seah, T. C. M., and Kaplan J. G.. 1973. Purification and properties of the catalase of bakers' yeast. J. Biol. Chem. 248:2889–2893.
   PubMedGoogle Scholar
• Shin, D. Y., Matsumoto K., Iida H., Uno I., and Ishikawa T.. 1987. Heat shock response of Saccharomyces cerevisiae mutants altered in cyclic AMP-dependent protein phosphorylation. Mol. Cell. Biol. 7:244–250.
   PubMed Web of Science ®Google Scholar
• Spevak, W., FessI F., Rytka J., Traczyk A., Skoneczny M., and Ruis H.. 1983. Isolation of the catalase T structural gene of Saccharomyces cerevisiae by functional complementation. Mol. Cell. Biol. 3:1545–1551.
   PubMedGoogle Scholar
• Spevak, W., Hartig A., Meindl P., and Ruis H.. 1986. Heme control region of the catalase T gene of the yeast Saccharomyces cerevisiae. Mol. Gen. Genet. 203:73–78.
   PubMedGoogle Scholar
• Susani, M., Zimniak P., Fessl F., and Ruis H.. 1976. Localization of catalase A in vacuoles of Saccharomyces cerevisiae: evidence for the vacuolar nature of isolated “yeast peroxisomes.” Hoppe-Seyler's Z. Physiol. Chem. 357:961–970.
   PubMedGoogle Scholar
• Tanaka, K., Matsumoto K., and Toh-e A.. 1988. Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast. EMBO J. 7:495–502.
   PubMedGoogle Scholar
• Tatchell, K.. 1986. RAS genes and growth control in Saccharomyces cerevisiae. J. Bacteriol. 166:364–367.
   PubMedGoogle Scholar
• Tatchell, K., Robinson L. C., and Breitenbach M.. 1989. RAS2 of Saccharomyces cerevisiae is required for gluconeogenic growth and proper response to nutrient limitation. Proc. Natl. Acad. Sci. USA 82:3785–3789.
   Google Scholar
• Thomas, P. S.. 1980. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA 77:5201–5205.
   PubMed Web of Science ®Google Scholar
• Toda, T., Cameron S., Sass P., Zoller M., Scott J. D., McMullen B., Hurwitz M., Krebs E. G., and Wigler M.. 1987. Cloning and characterization of BCY1, a locus encoding the regulatory subunit of the cyclic AMP-dependent protein kinase in Saccharomyces cerevisiae. Mol. Cell. Biol. 7:1371–1377.
   PubMed Web of Science ®Google Scholar
• Wilson, R. B., and Tatchell K.. 1988. SRA5 encodes the low-A:m cyclic AMP phosphodiesterase of Saccharomyces cerevisiae. Mol. Cell. Biol. 8:505–510.
   PubMedGoogle Scholar
• Winkler, H., Adam G., Mattes E., Schanz M., Hartig A., and Ruis H.. 1988. Co-ordinate control of synthesis of mitochondrial and non-mitochondrial hemoproteins: a binding site for the HAP1 (CYP1) protein in the UAS region of the yeast catalase T gene (C7T7). EMBO J. 7:1799–1804.
   PubMed Web of Science ®Google Scholar