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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Biotechnology 38 (1994), S. 81-88 
    ISSN: 0168-1656
    Keywords: Heterologous protein ; S. cerevisiae ; [abr] %PI(-); percentage of cells do not stain with propidium iodide ; [abr] ADC1; gene encoding the yeast alcohol dehydrogenase I (promoter) ; [abr] AP(CE); AP activity measured in the soluble protein cell extract ; [abr] AP(M); AP activity measured in the culture medium as U ml^-^1 ; [abr] BCK1/SLK1; gene encoding the yeast protein kinase Bck1/Slk1 ; [abr] CAT(CE); CAT activity measured in the soluble protein cell ; [abr] CAT(M); CAT activity measured in the culture medium as U ml^-^1 ; [abr] CYC1; gene encoding the yeast cytochrome oxidase I (terminator) ; [abr] MKK1/MKK2; genes encoding the yeast kinases Mkk1 and Mkk2 ; [abr] PEP4; gene encoding the yeast proteinase A ; [abr] PKC1; gene encoding the yeast kinase C ; [abr] PRB1; gene encoding the yeast proteinase B ; [abr] SLT2/MPK1; gene encoding the yeast MAP kinase homolog Slt2/Mpk1 ; slt2 mutant
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0983
    Keywords: Yeast ; SLT2 ; MAP-kinase ; Caffeine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have further characterized the functionality of theSaccharomyces cerevisiae geneSLT2(MPK1), coding for a MAP-kinase homolog essential for cell integrity, which is involved in the Pkc1p signalling pathway. This gene was isolated on the basis of its capacity to complement the thermosensitive-autolytic, osmotic-remediable phenotype oflyt2 mutants. Bothslt2A andlyt2 mutants displayed a caffeine-sensitive phenotype consisting of cell lysis that was not dependent on temperature. Caffeine concentrations affecting the growth of these mutant strains were dependent on the genetic background, theSSD1 allele being very significant in this regard. TheSLT2 allele of severallyt2 strains was both rescued and amplified by PCR. The recovered allele was shown to be non-functional as it could not complement the lytic phenotype of both deletion (slt2Δ) andlyt2 strains. After nucleotide sequencing of the recovered allele, we found that the defect oflyt2 mutants consists in a substitution of an aspartic acid for a glycine at position 35 of the amino-acid sequence of Slt2p. Gly35 is the third glycine of a glycine cluster (Gly-X-Gly-X-X-Gly), a conserved region in protein kinases and other nucleotide-binding proteins.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0983
    Keywords: Keywords Yeast ; SLT2 ; MAP-kinase ; Caffeine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We have further characterized the functionality of the Saccharomyces cerevisiae gene SLT2(MPK1), coding for a MAP-kinase homolog essential for cell integrity, which is involved in the Pkc1p signalling pathway. This gene was isolated on the basis of its capacity to complement the thermosensitive-autolytic, osmotic-remediable phenotype of lyt2 mutants. Both slt2Δ and lyt2 mutants displayed a caffeine-sensitive phenotype consisting of cell lysis that was not dependent on temperature. Caffeine concentrations affecting the growth of these mutant strains were dependent on the genetic background, the SSD1 allele being very significant in this regard. The SLT2 allele of several lyt2 strains was both rescued and amplified by PCR. The recovered allele was shown to be non-functional as it could not complement the lytic phenotype of both deletion (slt2Δ) and lyt2 strains. After nucleotide sequencing of the recovered allele, we found that the defect of lyt2 mutants consists in a substitution of an aspartic acid for a glycine at position 35 of the amino-acid sequence of Slt2p. Gly35 is the third glycine of a glycine cluster (Gly-X-Gly-X-X-Gly), a conserved region in protein kinases and other nucleotide-binding proteins.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 121 (1979), S. 265-270 
    ISSN: 1432-072X
    Keywords: 1,6-β-Glucanase ; Characterization ; Catabolite repression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The filamentous fungus Penicillium italicum when grown in a synthetic medium, produced and secreted 1,6-β-glucanase into the culture medium. This enzyme has been partially purified by gel filtration. After this step the active fractions were free of 1,3-β-glucanase, α-amylase and β-glucosidase activities. Only four proteins, one associated with the enzyme, were found by polyacrylamide gel electrophoresis under non denaturing conditions. The enzyme behaves as an acidic protein (pI 4.65) with an optimum pH of 5 and an endohydrolytic mode of action. The activity was lost at pHs greater than 7. The enzyme was also found associated with the mycelium. Its synthesis was repressed by glucose or growth-promoting sugars. Derepression in low glucose containing medium required protein synthesis. 8-Hydroxyquinoline, an RNA synthesis inhibitor, added during the derepression period did permit some increase in the specific activity but prevented it when added at the beginning of that period.
    Type of Medium: Electronic Resource
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