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  • 1
    Electronic Resource
    Electronic Resource
    Growth of catalase A and catalase T deficient mutant strains of Saccharomyces cerevisiae on ethanol and oleic acid (1990)
    Springer
    Archives of microbiology 153 (1990), S. 513-517 
    Details
    ISSN: 1432-072X
    Keywords: Saccharomyces cerevisiae ; Catalase A ; Catalase T ; β-Oxidation ; Microbodies ; H2O2-Metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The parental strain (A+T+) of Saccharomyces cerevisiae and mutants, deficient in catalase T (A+T−), catalase A (A−T+) or both catalases (A−T−), grew on ethanol and oleic acid with comparable doubling times. Specific activities of catalase were low in glucose- and ethanol-grown cells. In the two oleic acid-grown A+-strains (A+T+ and A+T−) high catalase activities were found; catalase activity invariably remained low in the A−T+ strain and was never detected in the A−T− strain. The levels of β-oxidation enzymes in oleic acid-grown cells of the parental and all mutant strains were not significantly different. However, cytochrome C peroxidase activity had increased 8-fold in oleic acid grown A− strains (A−T+ and A−T−) compared to parental strain cells. The degree of peroxisomal proliferation was comparable among the different strains. Catalase A was shown to be located in peroxisomes. Catalase T is most probably cytosolic in nature and/or present in the periplasmic space.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248436
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  • 2
    Electronic Resource
    Electronic Resource
    The deficiency of sterol biosynthesis in Saccharomyces cerevisiae affects the synthesis of glycosyl derivatives of dolichyl phosphates (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 112 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Mutants deficient in sterol (thermosensitive ergosterol auxotrophs) erg 8, 9, 12 and heme synthesis hem 1, 12 were screened for the level of free dolichol and dolichyl phosphate synthesized in the mevalonate pathway as well as for the activity of dolichyl phosphate-dependent glycosyl transferases. The amount of DolP synthesized via CTP-dependent phosphorylation was the same in mutants and parental strains. However, mannosylation and glucosylation of endogenous dolichyl phosphates in ergosterol mutants was about four times lower compared to parental strains, while the same reactions carried out with exogenous Dol24P reached 80% of the level observed in parental strains indicating that activities of DolPMan and DolPGlc synthases are not the rate-limiting factors. It is postulated that the de novo synthesis of DolP is impaired in the ergosterol mutants. Moreover, a block in the ergosterol branch of the metabolic pathway (erg 9) causes an increase in the de novo synthesis of dolichyl phosphate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06470.x
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  • 3
    Electronic Resource
    Electronic Resource
    The bromodomain-containing protein Bdf1p acts as a phenotypic and transcriptional multicopy suppressor of YAF9 deletion in yeast (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 53 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: It was observed previously that the deletion of the open reading frame YNL107w (YAF9) was highly pleiotropic in yeast and caused defective growth phenotypes in the presence of several unrelated inhibitors, including caesium chloride. We have selected multicopy extragenic suppressor genes, revealing that this phenotype can be suppressed by overdosing the transcription factors BDF1 and GAT1 in the yaf9Δ strain. We focused our analysis on suppression by BDF1 and performed a genome-wide transcript analysis on a yaf9Δ strain, compared with the wild-type and BDF1-suppressed strains. YAF9 deletion has a clear effect on transcription and leads to modulation of the level of expression of several genes. Transcription of a considerable portion of the underexpressed genes is restored to wild-type levels in the BDF1-suppressed strain. We show by chromatin immunoprecipitation that both Yaf9p and Bdf1p bind to promoters of some of these genes and that the level of H3 and H4 acetylation at one of these promoters is significantly lowered in the yaf9 deleted strain, compared with the wild-type and the BDF1-suppressed strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04184.x
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  • 4
    Electronic Resource
    Electronic Resource
    Posttranscriptional heme control of catalase synthesis in the yeast Saccharomyces cerevisiae (1981)
    Springer
    Current genetics 4 (1981), S. 19-23 
    Details
    ISSN: 1432-0983
    Keywords: Catalase ; Saccharomyces cerevisiae ; Heme ; Posttranscriptional control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Compared to wild type cells, strains bearing the pleiotropic regulatory mutations cgr4 or cas1 synthesize apocatalase T at a high rate when grown on high glucose. Like heme-deficient ole3 single mutants, ole3 cgr4 and ole3 cas1 double mutants accumulate no catalase T protein in vivo. This defect introduced by the ole3 mutation is cured by the addition of ALA. By use of the inhibitor actinomycin D we confirm previous findings that ole3 mutants lack catalase T mRNA and show that (i) the ole3 cgr4 and ole3 cas1 double mutants do accumulate catalase T mRNA or mRNA precursor, and (ii) the processing or translation of this RNA or the accumulation of apocatalase T depends on the presence of home.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00376781
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the cta1 mutation (1985)
    Springer
    Molecular genetics and genomics 200 (1985), S. 74-79 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary As a first step in an analysis of the DNA regions involved in the control of the catalase A gene of Saccharomyces cerevisiae by glucose, heme, and oxygen this gene has been cloned. Catalase A-deficient mutants were obtained by UV mutagenesis of a ctt1 mutant strain specifically lacking catalase T. All the catalase A-deficient mutants obtained fall into one complementation group. The single recessive mutation causing specific lack of catalase A was designated cta1. Several overlapping DNA fragments complementing the cta1 mutation were obtained by transforming ctt1 cta1 double mutants with a yeast gene library in vector YEp13. Hybrid selection of RNA with the help of one of the cloned DNAs followed by in vitro translation of this RNA and identification of the protein synthesized with catalase A-specific antibodies showed that the catalase A structural gene has been cloned. A single copy of this gene is present in the yeast genome. Transcription of the catalase A gene cloned into vector YEp13 is repressed by glucose. The DNA isolated hybridizes to a 1.6 kb polyA+−RNA virtually absent from heme-deficient cells, presumably catalase A mRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00383315
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  • 6
    Electronic Resource
    Electronic Resource
    Analysis of heme biosynthesis in catalase and cytochrome deficient yeast mutants (1977)
    Springer
    Molecular genetics and genomics 156 (1977), S. 177-183 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutants of Saccharomyces cerevisiae, described as catalase and cytochromes deficient (Pachecka et al., 1974), have been analyzed for heme biosynthesis ability. Some enzymatic activities involved in protoheme synthesis were measured in acellular extracts, whereas whole cells were analyzed for cytochrome spectra and for possible accumulation of porphyrin synthesis intermediates. A good correlation was found between these in vitro and in vivo studies. Results show that two mutants were impaired in 5-aminolevulinate synthesis, two mutants were devoid of uroporphyrinogen I synthetase activity and one mutant presented defects in coproporphyrinogen III oxidase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00283490
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  • 7
    Electronic Resource
    Electronic Resource
    Haemoprotein formation in yeast (1978)
    Springer
    Molecular genetics and genomics 160 (1978), S. 51-57 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Catalase A and T activities were investigated in two standard strains and three catalase regulatory cgr mutants of yeast in respiratory competent and incompetent states, which were under various degrees of glucose repression. The formation of catalase A was very sensitive to glucose repression and was characterized by a long delay in derepression. Deprivation of the energy source in respiratory incompetent cells prevented the derepression of catalase A. The lack of catalase A in respiratory incompetent cells can be overcome by growing the cells in raffinose or by the prolongation of the fermentative phase of derepression. Catalase T is under control of different regulatory systems probably common with some other haemoproteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00275118
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  • 8
    Electronic Resource
    Electronic Resource
    Haemoprotein formation in yeast (1976)
    Springer
    Molecular genetics and genomics 145 (1976), S. 37-42 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A procedure was described for the isolation of mutants affected in the regulation of catalase activity. Two such mutants, cgr 1 and cgr 2 were obtained. Both of them show catalase activity that is resistant to repression by glucose, but is sensitive to anoxia to the same extent as the wild type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331555
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  • 9
    Electronic Resource
    Electronic Resource
    Isolation and characterization of extragenic mutations affecting the expression of the uroporphyrinogen decarboxylase gene (HEM12) in Sacharomyces cerevisiae (1995)
    Springer
    Molecular genetics and genomics 247 (1995), S. 471-481 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Uroporphyrinogen decarboxylase ; HEM12 transcription ; Porphyria cutanea tarda
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Uroporphyrinogen decarboxylase (Uro-d; EC 4.1.1.37), the fifth enzyme in the heme biosynthetic pathway, which catalyzes the sequential decarboxylation of uroporphyrinogen to coproporphyrinogen, is encoded by the HEM12 gene in Saccharomyces cerevisiae. The HEM12 gene is transcribed into a major short mRNA and a minor longer one, approximately 1.35 and 1.55 kb, respectively, in size, and that differ in the 5′ untranslated region. “Uroporphyric” mutants, which have no mutations in the HEM12 gene but accumulate uroporphyrinogen, a phenotype chracteristic of partial Uro-d deficiency, were investigated. Genetic analysis showed that the mutant phenotype depends on the combined action of two unlinked mutations, udt1 and either ipa1, ipa2, or ipa3. ipa1 is tightly linked to HEM12 The mutation udt1 apparently acts specifically on the HEM12 gene, and causes a six to tenfold decrease in the levels of the short HEM12 mRNA, in the β-galactosidase activity of a HEM12-lacZ fusion, in immunodetectable protein and enzyme activity. But heme synthesis is normal and porphyrin accumulation was modest. The mutations ipa1, ipa2, and ipa3 had no phenotype on their own, but they caused an increase in porphyrin accumulation in a udt1 background. This multiplicity of genetic factors leading to uroporphyric yeast cells closely resembles the situation in human porphyria cutanea tarda.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293149
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  • 10
    Electronic Resource
    Electronic Resource
    A new essential gene located on Saccharomyces cerevisiae chromosome IX (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 885-890 
    Details
    ISSN: 0749-503X
    Keywords: new essential gene ; chromosome IX ; RBP1 ; adenylate cyclase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A new 1150 amino acids long open reading frame (ORF), coding for an essential protein of unknown function was found Saccharomyces cerevisiae by sequencing 3754 bp of geonomic DNA. The clone was isolated in a search for a fatty acid-binding protein (FABP) and was localized on chromosome IX. The ORF bears no homology to FABP, but it shows weak similarity to Plasmodium vivax reticulocyte binding protein 1 and to aggregation-specific adenylate cyclase from Dictyostelium discoideum. The new gene is constitutively transcribed regardless of the carbon source used. The nucleotide sequence reported in this paper has been deposited in GenBank (Accession Number U17918).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320110910
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