Abstract
Transcription of the CTT1 (catalase T) gene of Saccharomyces cerevisiae is controlled by oxygen via heme, by nutrients via cAMP and by heat shock. Nitrogen limitation triggers a rapid, cycloheximide-insensitive derepression of the gene. Residual derepression in a cAMP-nonresponsive mutant with attenuated protein kinase activity (bcy1 tpk1w tpk2 tpk3) demonstrates the existence of an alternative, cAMP-independent nutrient signaling mechanism. Deletion analysis using CTT1-lacZ fusion genes revealed the contribution of multiple control elements to derepression, not all of which respond to the cAMP signal. A positive promoter element responding to negative control by cAMP was inactivated by deletion of a DNA region between base pairs -340 and -364. Upstream fragments including this element confer negative cAMP control to a LEU2-lacZ fusion gene. Northern analysis of CTT1 expression in the presence or absence of heme, in RAS2+ (high cAMP) and ras2 mutant (low cAMP) strains and in cells grown at low temperature (23 degrees C) and in heat-shocked cells (37 degrees C) shows that CTT1 is only induced to an appreciable extent when at least two of the three factors contributing to its expression (oxidative stress signaled by heme, nutrient starvation (low cAMP) and heat stress) activate the CTT1 promoter.
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Selected References
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- Amin J., Ananthan J., Voellmy R. Key features of heat shock regulatory elements. Mol Cell Biol. 1988 Sep;8(9):3761–3769. doi: 10.1128/mcb.8.9.3761. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BEERS R. F., Jr, SIZER I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952 Mar;195(1):133–140. [PubMed] [Google Scholar]
- Beggs J. D. Transformation of yeast by a replicating hybrid plasmid. Nature. 1978 Sep 14;275(5676):104–109. doi: 10.1038/275104a0. [DOI] [PubMed] [Google Scholar]
- Bissinger P. H., Wieser R., Hamilton B., Ruis H. Control of Saccharomyces cerevisiae catalase T gene (CTT1) expression by nutrient supply via the RAS-cyclic AMP pathway. Mol Cell Biol. 1989 Mar;9(3):1309–1315. doi: 10.1128/mcb.9.3.1309. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Boorstein W. R., Craig E. A. Regulation of a yeast HSP70 gene by a cAMP responsive transcriptional control element. EMBO J. 1990 Aug;9(8):2543–2553. doi: 10.1002/j.1460-2075.1990.tb07435.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
- Cameron S., Levin L., Zoller M., Wigler M. cAMP-independent control of sporulation, glycogen metabolism, and heat shock resistance in S. cerevisiae. Cell. 1988 May 20;53(4):555–566. doi: 10.1016/0092-8674(88)90572-7. [DOI] [PubMed] [Google Scholar]
- Cannon J. F., Gibbs J. B., Tatchell K. Suppressors of the ras2 mutation of Saccharomyces cerevisiae. Genetics. 1986 Jun;113(2):247–264. doi: 10.1093/genetics/113.2.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cannon J. F., Gitan R., Tatchell K. Yeast cAMP-dependent protein kinase regulatory subunit mutations display a variety of phenotypes. J Biol Chem. 1990 Jul 15;265(20):11897–11904. [PubMed] [Google Scholar]
- Cherry J. R., Johnson T. R., Dollard C., Shuster J. R., Denis C. L. Cyclic AMP-dependent protein kinase phosphorylates and inactivates the yeast transcriptional activator ADR1. Cell. 1989 Feb 10;56(3):409–419. doi: 10.1016/0092-8674(89)90244-4. [DOI] [PubMed] [Google Scholar]
- Cohen G., Fessl F., Traczyk A., Rytka J., Ruis H. Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the cta1 mutation. Mol Gen Genet. 1985;200(1):74–79. doi: 10.1007/BF00383315. [DOI] [PubMed] [Google Scholar]
- Eisen A., Taylor W. E., Blumberg H., Young E. T. The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2. Mol Cell Biol. 1988 Oct;8(10):4552–4556. doi: 10.1128/mcb.8.10.4552. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hartig A., Ruis H. Nucleotide sequence of the Saccharomyces cerevisiae CTT1 gene and deduced amino-acid sequence of yeast catalase T. Eur J Biochem. 1986 Nov 3;160(3):487–490. doi: 10.1111/j.1432-1033.1986.tb10065.x. [DOI] [PubMed] [Google Scholar]
- Hörtner H., Ammerer G., Hartter E., Hamilton B., Rytka J., Bilinski T., Ruis H. Regulation of synthesis of catalases and iso-1-cytochrome c in Saccharomyces cerevisiae by glucose, oxygen and heme. Eur J Biochem. 1982 Nov;128(1):179–184. doi: 10.1111/j.1432-1033.1982.tb06949.x. [DOI] [PubMed] [Google Scholar]
- Ito H., Fukuda Y., Murata K., Kimura A. Transformation of intact yeast cells treated with alkali cations. J Bacteriol. 1983 Jan;153(1):163–168. doi: 10.1128/jb.153.1.163-168.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Luche R. M., Sumrada R., Cooper T. G. A cis-acting element present in multiple genes serves as a repressor protein binding site for the yeast CAR1 gene. Mol Cell Biol. 1990 Aug;10(8):3884–3895. doi: 10.1128/mcb.10.8.3884. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsumoto K., Uno I., Ishikawa T. Genetic analysis of the role of cAMP in yeast. Yeast. 1985 Sep;1(1):15–24. doi: 10.1002/yea.320010103. [DOI] [PubMed] [Google Scholar]
- Matsuura A., Treinin M., Mitsuzawa H., Kassir Y., Uno I., Simchen G. The adenylate cyclase/protein kinase cascade regulates entry into meiosis in Saccharomyces cerevisiae through the gene IME1. EMBO J. 1990 Oct;9(10):3225–3232. doi: 10.1002/j.1460-2075.1990.tb07521.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ozkaynak E., Finley D., Solomon M. J., Varshavsky A. The yeast ubiquitin genes: a family of natural gene fusions. EMBO J. 1987 May;6(5):1429–1439. doi: 10.1002/j.1460-2075.1987.tb02384.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Praekelt U. M., Meacock P. A. HSP12, a new small heat shock gene of Saccharomyces cerevisiae: analysis of structure, regulation and function. Mol Gen Genet. 1990 Aug;223(1):97–106. doi: 10.1007/BF00315801. [DOI] [PubMed] [Google Scholar]
- Richter K., Ammerer G., Hartter E., Ruis H. The effect of delta-aminolevulinate on catalase T-messenger RNA levels in delta-aminolevulinate synthase-defective mutants of Saccharomyces cerevisiae. J Biol Chem. 1980 Sep 10;255(17):8019–8022. [PubMed] [Google Scholar]
- Rose M., Botstein D. Construction and use of gene fusions to lacZ (beta-galactosidase) that are expressed in yeast. Methods Enzymol. 1983;101:167–180. doi: 10.1016/0076-6879(83)01012-5. [DOI] [PubMed] [Google Scholar]
- Sarokin L., Carlson M. Upstream region of the SUC2 gene confers regulated expression to a heterologous gene in Saccharomyces cerevisiae. Mol Cell Biol. 1985 Oct;5(10):2521–2526. doi: 10.1128/mcb.5.10.2521. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Seah T. C., Bhatti A. R., Kaplan J. G. Novel catalatic proteins of bakers' yeast. I. An atypical catalase. Can J Biochem. 1973 Nov;51(11):1551–1555. doi: 10.1139/o73-208. [DOI] [PubMed] [Google Scholar]
- Seah T. C., Kaplan J. G. Purification and properties of the catalase of bakers' yeast. J Biol Chem. 1973 Apr 25;248(8):2889–2893. [PubMed] [Google Scholar]
- Shin D. Y., Matsumoto K., Iida H., Uno I., Ishikawa T. Heat shock response of Saccharomyces cerevisiae mutants altered in cyclic AMP-dependent protein phosphorylation. Mol Cell Biol. 1987 Jan;7(1):244–250. doi: 10.1128/mcb.7.1.244. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Skoneczny M., Chełstowska A., Rytka J. Study of the coinduction by fatty acids of catalase A and acyl-CoA oxidase in standard and mutant Saccharomyces cerevisiae strains. Eur J Biochem. 1988 Jun 1;174(2):297–302. doi: 10.1111/j.1432-1033.1988.tb14097.x. [DOI] [PubMed] [Google Scholar]
- Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
- Spevak W., Fessl F., Rytka J., Traczyk A., Skoneczny M., Ruis H. Isolation of the catalase T structural gene of Saccharomyces cerevisiae by functional complementation. Mol Cell Biol. 1983 Sep;3(9):1545–1551. doi: 10.1128/mcb.3.9.1545. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spevak W., Hartig A., Meindl P., Ruis H. Heme control region of the catalase T gene of the yeast Saccharomyces cerevisiae. Mol Gen Genet. 1986 Apr;203(1):73–78. doi: 10.1007/BF00330386. [DOI] [PubMed] [Google Scholar]
- Struhl K., Stinchcomb D. T., Scherer S., Davis R. W. High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1035–1039. doi: 10.1073/pnas.76.3.1035. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tanaka K., Matsumoto K., Toh-e A. Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast. EMBO J. 1988 Feb;7(2):495–502. doi: 10.1002/j.1460-2075.1988.tb02837.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tatchell K., Chaleff D. T., DeFeo-Jones D., Scolnick E. M. Requirement of either of a pair of ras-related genes of Saccharomyces cerevisiae for spore viability. Nature. 1984 Jun 7;309(5968):523–527. doi: 10.1038/309523a0. [DOI] [PubMed] [Google Scholar]
- Tatchell K., Nasmyth K. A., Hall B. D., Astell C., Smith M. In vitro mutation analysis of the mating-type locus in yeast. Cell. 1981 Nov;27(1 Pt 2):25–35. doi: 10.1016/0092-8674(81)90357-3. [DOI] [PubMed] [Google Scholar]
- Tatchell K. RAS genes and growth control in Saccharomyces cerevisiae. J Bacteriol. 1986 May;166(2):364–367. doi: 10.1128/jb.166.2.364-367.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Werner-Washburne M., Becker J., Kosic-Smithers J., Craig E. A. Yeast Hsp70 RNA levels vary in response to the physiological status of the cell. J Bacteriol. 1989 May;171(5):2680–2688. doi: 10.1128/jb.171.5.2680-2688.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Winkler H., Adam G., Mattes E., Schanz M., Hartig A., Ruis H. 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 (CTT1). EMBO J. 1988 Jun;7(6):1799–1804. doi: 10.1002/j.1460-2075.1988.tb03011.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Xiao H., Lis J. T. Germline transformation used to define key features of heat-shock response elements. Science. 1988 Mar 4;239(4844):1139–1142. doi: 10.1126/science.3125608. [DOI] [PubMed] [Google Scholar]