Novel Catalatic Proteins of Bakers' Yeast. I. An Atypical Catalase

Seah, Tony C.M.; Bhatti, A. R.; Kaplan, Joseph

doi:10.1139/o73-208

Cited by 59 publications

(27 citation statements)

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“…1) Extracts from cells transformed with plasmid hybridized to YEp13-51 lacked catalase T activity completely, d were phos-whereas the transformants clearly showed cataumin (69,000), lase activity in a colony test. From this finding, drase (30,000). it was tentatively concluded that this plasmid nd catalase A, contains an incomplete catalase T gene coding for an altered catalase T protein that is sufficiently stable in intact cells but unstable in {as bound to extracts.…”

Section: Resultsmentioning

confidence: 76%

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Isolation of the catalase T structural gene of Saccharomyces cerevisiae by functional complementation.

Spevak¹,

Fessl²,

Rytka³

et al. 1983

Mol. Cell. Biol.

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The catalase T structural gene of Saccharomyces cerevisiae was cloned by functional complementation of a mutation causing specific lack of the enzyme (cttl). Catalase T-deficient mutants were obtained by UV mutagenesis of an S. cerevisiae strain bearing the cas1 mutation, which causes insensitivity of catalase T to glucose repression. Since the second catalase protein of S. cerevisiae, catalase A, is completely repressed on 10% glucose, catalase T-deficient mutant colonies could be detected under such conditions. A cttl mutant was transformed with an S. cerevisiae gene library in plasmid YEp13. Among the catalase T-positive clones, four contained overlapping DNA fragments according to restriction analysis. Hybridization selection of yeast mRNA binding specifically to one of the cloned DNAs, translation of this mRNA in cell-free protein synthesis systems, and demonstration of catalase T protein formation by specific immunoadsorption showed that the catalase T structural gene had been cloned. By subcloning, the gene was located within a 3.5-kilobase S. cerevisiae DNA fragment. As in wild-type cells, catalase T synthesis in cttl mutant cells transformed with plasmids containing this fragment is sensitive to glucose repression. By DNA-RNA hybridization, catalase T transcripts were shown to be present in oxygen-adapting cells but absent from heme-deficient cells.

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Section: Resultsmentioning

confidence: 76%

“…The yeast Saccharomyces cerevisiae contains two main catalase proteins called catalase T and catalase A (30,31). The regulation of these proteins by glucose, oxygen, and heme, their prosthetic group, has been studied by translation in vitro of total yeast mRNA and immunological detection of catalase proteins synthesized by the cell-free system (17,26).…”

mentioning

confidence: 99%

Isolation of the catalase T structural gene of Saccharomyces cerevisiae by functional complementation.

Spevak¹,

Fessl²,

Rytka³

et al. 1983

Mol. Cell. Biol.

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“…In Saccharomyces cerevisiae cells, two different types of catalase have been found (Traczyk et al 1985;Skoneczny and Rytka, 2000), which were designated catalase type A and catalase type T * Corresponding autor (Seah et al 1973). The two enzymes are encoded by different genes (CTA1 and CTT1 respectively), possessing independent control and being localized in different compartments: catalase T is a cytoplasm enzyme whereas catalase A is localized in peroxisomes (Lapinskas et al 1993).…”

mentioning

confidence: 99%

Efficient transformation of Penicillium chrysogenum mediated by Agrobacterium tumefaciens LBA4404 for cloning of Vitreoscilla hemoglobin gene

Sun¹,

Qiu-lian²,

Xu³

2002

Electron. J. Biotechnol.

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“…The yeast Saccharomyces cerevisiae contains two different hemoprotein catalases, the peroxisomal catalase A (32), which is encoded by the CTAI gene (11), and the cytoplasmic catalase T (33), encoded by CTTJ (35). Like the CYC1 (iso-1-cytochrome c) gene, the two catalase genes have been reported to be controlled positively by oxygen and hence and negatively by glucose repression (18).…”

mentioning

confidence: 99%

Control of Saccharomyces cerevisiae catalase T gene (CTT1) expression by nutrient supply via the RAS-cyclic AMP pathway.

Bissinger¹,

Wieser²,

Hamilton³

et al. 1989

Mol. Cell. Biol.

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In Saccharomyces cerevisiae, lack of nutrients triggers a pleiotropic response characterized by accumulation of storage carbohydrates, early Gl arrest, and sporulation of a/at diploids. This response is thought to be mediated by RAS proteins, adenylate cyclase, and cyclic AMP (cAMP)-dependent protein kinases. This study shows that expression of the S. cerevisiae gene coding for a cytoplasmic catalase T (CTTI) is controlled by this pathway: it is regulated by the availability of nutrients. For growth on STMD2%, cells grown on YPD2% plates or in liquid YPD2% were transferred to STMD2% (optical density at 600 nm, 1.0) and were incubated at 30°C for 36 h (after this period, all cells were arrested unbudded in early Gl). Synthetic a-factor (kindly provided by K; Nasmyth) was added in some experiments to a final concentration of 0. 1 p.g per ml of culture. Cells were grown and incubated on SM in the same way as on STMD2%. Strains bearing cdc mutations were pregrown at 23°C on YPD2% to an optical density at 600 nm of 2.5, and the cultures were divided, transferred to STMD2% in some experiments, and incubated for 5 h at 23 and 35°C on YPD2% or STMD2%, respectively, before being harvested.Enzyme activities. The specific activity of ,-galactosidase of crude extracts from yeast strains bearing a single-copy CTTI-lacZ fusion gene (36) integrated into the chromosomal URA3 locus (see Fig. 1) was assayed as described by Miller (26).

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Novel Catalatic Proteins of Bakers' Yeast. I. An Atypical Catalase

Cited by 59 publications

References 0 publications

Isolation of the catalase T structural gene of Saccharomyces cerevisiae by functional complementation.

Isolation of the catalase T structural gene of Saccharomyces cerevisiae by functional complementation.

Efficient transformation of Penicillium chrysogenum mediated by Agrobacterium tumefaciens LBA4404 for cloning of Vitreoscilla hemoglobin gene

Control of Saccharomyces cerevisiae catalase T gene (CTT1) expression by nutrient supply via the RAS-cyclic AMP pathway.

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