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  • 1
    Electronic Resource
    Electronic Resource
    The proteolytic system of the fission yeast Schizosaccharomyces pombe (1991)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 81 (1991), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: Proteinase and peptidase activities of the fission yeast Schizosaccharomyces pombe were investigated. Several intracellular proteolytic enzymes were found: two endoproteinases, one carboxypeptidase, one aminopeptidase and one dipeptidyl-aminopeptidase. In addition, proteinase inhibitors were detected. In fresh crude extracts an activation procedure is needed to measure maximal activities of endoproteinases and carboxypeptidase, whose level is markedly dependent on growth medium composition and on growth phase, while aminopeptidase and dipeptidyl-aminopeptidase activities are very little, if at all, regulated by the carbon source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04748.x
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  • 2
    Electronic Resource
    Electronic Resource
    Regulation of the yeast vacuolar aminopeptidase Y gene (APY1) expression (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 139 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The steady-state levels of the aminopeptidase Y (APY1) transcript and the levels of assayable aminopeptidase Y activity were measured under a variety of nutritional conditions. Specific APY1 mRNA is less abundant in cells grown in minimal medium than in cells grown in rich medium, while active enzyme levels follow just the opposite pattern. Aminopeptidase Y activity decreases when cells are deprived of glucose without a concomitant fall in mRNA levels. Production of aminopeptidase Y is not markedly affected by nitrogen regulation. APY1 gene expression is not disturbed in heat-shocked cells. Our data support the idea that the main control event in vacuolar aminopeptidase Y expression is a post-transcriptional step.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08191.x
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  • 3
    Electronic Resource
    Electronic Resource
    Dipeptidyl aminopeptidase yspI mutants of Schizosaccharomyces pombe: Genetic mapping of dpa1+ on chromosome III (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 120 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A mutant strain of Schizosaccharomyces pombe lacking dipeptidyl aminopeptidase yspI was isolated from a strain already defective in aminopeptidase activity by means of a staining technique with the chromogenic substrate ala-pro-4-methoxy-β-naphthylamide to screen colonies for the absence of the enzyme. The defect segregated 2+ :2− in meiotic tetrads, indicating a single chromosomal gene mutation, which was shown to be recessive. Gene dosage experiments indicated that the mutation resides in the structural gene of dipeptidyl aminopeptidase yspI, dpa1+. The dpa1+ gene was located on chromosome III by using l m- fluorophen-ylalanine-induced haploidization and mitotic analysis. dpa1 mutants did not show any obvious phenotype under a variety of conditions tested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07033.x
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  • 4
    Electronic Resource
    Electronic Resource
    Cis and trans-acting regulatory elements required for regulation of the CPS1 gene in Saccharomyces cerevisiae (1995)
    Springer
    Molecular genetics and genomics 246 (1995), S. 580-589 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Gene regulation ; Carboxypeptidase yscS ; Vacuolar peptidase ; Regulatory elements
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To clarify the transcriptional regulation by nutrient limitation of the gene encoding carboxypeptidase yscS in Saccharomyces cerevisiae (CPS1), we performed an analysis of its 5′ noncoding region. In deletion experiments a sequence located between positions −644 and −591 was found to be responsible for transcriptional repression of the CPS1 gene in yeast cells grown on rich nitrogen sources. Furthermore, a 162 bp fragment spanning positions −644 to −482 of the promoter of the CPS1 gene repressed gene expression when placed 3′ to the upstream activation sequence (UAS) of the heterologous gene CYC1. A fragment containing this putative upstream repression sequence (URS) was shown specifically to bind protein from a yeast extract as demonstrated by gel retardation experiments. Although a sequence mediating the control of gene expression by GCN4 was found within the URS element, the GCN4 gene product is not required for DNA-binding activity. In addition, at least three other upstream activation UASs responsible for the activation of CPS1 expression by glucose under nitrogen starvation conditions were found to be located between positions −673 and −644, −482 and −353, and −243 and −186, respectively. The putative mechanism of the nitrogen limitation-dependent regulation of CPS1 expression via these regulatory elements is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00298964
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  • 5
    Electronic Resource
    Electronic Resource
    Vacuolar carboxypeptidase Y of Saccharomyces cerevisiae is glycosylated, sorted and matured in the fission yeast Schizosaccharomyces pombe (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 271-282 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; carboxypeptidase Y ; Saccharomyces cerevisiae ; Schizosaccharomyces pombe ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Vacuolar carboxypeptidase Y of Saccharomyces cerevisiae (CPYsc) has been expressed in a Schizosaccharomyces pombe strain devoid of the endogenous equivalent peptidase, employing a 2 μ derived plasmid. Immunoblot analysis revealed that CPYsc produced in the fission yeast has a higher molecular mass than mature CPYsc produced by the budding yeast. CPYsc is glycosylated when expressed in S. pombe and uses four N-linked glycosylation sites as shown by endoglycosidase H digestion. Carbohydrate removal leads to a protein moiety which is indistinguishable in size from deglycosylated CPYsc produced by S. cerevisiae. CPYsc isolated from S. pombe soluble extracts is enzymatically active and thus is presumed to undergo correct proteolytic maturation. Subcellular fractionation experiments showed a cofractionation of CPYsc with the S. pombe endoproteinases PrA and PrB, suggesting that the protein is correctly sorted to the vacuole and that these peptidases might be responsible for zymogen activation.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320110309
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  • 6
    Electronic Resource
    Electronic Resource
    Isolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activity (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 525-531 
    Details
    ISSN: 0749-503X
    Keywords: Fission yeast ; aminopeptidase ; mutant ; peptidase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A mutant strain of the fission yeast Schizosaccharomyces pombe defective in aminopeptidase I was isolated by screening for lack of activity against the chromogenic substrate lysine-β-naphthlamide in isolated colonies. Tetrad dissection of sporulated diploids heterozygous for the wild-type and mutant allele resulted in a 2:2 segregation of mutant and wild-type phenotype indicating a single chromosomal gene mutation. Gene dosage experiments indicated that the mutation might reside in the structural gene of aminopeptidase I. No vital consequences of aminopeptidase I deficiency on cell life and sporulation could be detected. However, the enzyme seems to be involved in protein degradation under conditions of nutrient deprivation.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320070512
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  • 7
    Electronic Resource
    Electronic Resource
    Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 637-644 
    Details
    ISSN: 0749-503X
    Keywords: Fission yeast ; aminopeptidase ; yeast peptidase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Aminopeptidase yspI was purified to apparent homogeneity from the fission yeast Schizosaccharomyces pombe. The molecular mass of the native enzyme was estimated to be 184 kDa by gel filtration chromatography. A value of 92 kDa was calculated after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is thus a dimer with two identical subunits. Optimum pH for cleavage of synthetic aminoacyl-4-nitroanilides is 7·0. Mercury ions, EDTA and chloroquine were found to be potent inhibitors of aminopeptidase yspI activity. Substrate specificity studies indicate that the purified enzyme cleaves L-lysine-4-nitroanilide with high efficiency.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090610
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  • 8
    Electronic Resource
    Electronic Resource
    Control of Saccharomyces cerevisiae carboxypeptidase S (CPS1) gene expression under nutrient limitation (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 339-349 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; peptidase ; nitrogen catabolite repression ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Expression of the vacuolar carboxypeptidase S (CPS1) gene in Saccharomyces cerevisiae is regulated by the availability of nutrients. Enzyme production is sensitive to nitrogen catabolite repression; i.e. the presence of ammonium ions maintains expression of the gene at a low level. Transfer of ammonium-glucose pre-grown cells to a medium deprived of nitrogen causes a drastic increase in CPS1 RNA level provided that a readily usable carbon source, such as glucose or fructose, is available to the cells. Derepression of the gene by nitrogen limitation is cycloheximide-insensitive. Neither glycerol, ethanol, acetate nor galactose support derepression of CPS1 expression under nitrogen starvation conditions. Non-metabolizable sugar analogs (2-deoxyglucose, 6-methyl-glucose or glucosamine) do not allow derepression of CPS1, showing that the process is energy-dependent. Production of carboxypeptidase yscS also increases several-fold when ammonium-pregrown cells are transferred to media containing glucose and a non-readily metabolizable nitrogen source such as proline, leucine, valine or leucyl-glycine. Analysis of CPS1 expression in RAS2+ (high cAMP) and ras2 mutant (low cAMP) strains and in cells grown at low temperature (23°C) and in heat-shocked cells (38°C) shows that steady-state levels of CPS1 mRNA are not controlled by a low cAMP level-signalling pathway.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090404
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  • 9
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    Molecular cloning and sequencing of genomic DNA encoding yeast vacuolar carboxypeptidase yscS (1991)
    Wiley
    Details
    Publication Date: 1991-05-20
    Print ISSN: 0014-5793
    Electronic ISSN: 1873-3468
    Topics: Biology , Chemistry and Pharmacology
    Published by Wiley on behalf of Federation of European Biochemical Societies.
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  • 10
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    Identification of regulatory proteins that might be involved in carbon catabolite repression of the aminopeptidase I gene of the yeast Saccharomyces cerevisiae (1995)
    Wiley
    Details
    Publication Date: 1995-11-27
    Print ISSN: 0014-5793
    Electronic ISSN: 1873-3468
    Topics: Biology , Chemistry and Pharmacology
    Published by Wiley on behalf of Federation of European Biochemical Societies.
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