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  • yeast  (4)
  • Springer  (2)
  • Wiley-Blackwell  (2)
  • Elsevier
  • Institute of Physics
  • 1
    Electronic Resource
    Electronic Resource
    Phosphatidate Phosphatase—A Key Enzyme in Glycerolipid Biosynthesis. Studies on the Yeast Enzyme (1998)
    Springer
    The protein journal 17 (1998), S. 1-7 
    Details
    ISSN: 1573-4943
    Keywords: Phosphatidate phosphatase ; purification ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Phosphatidate phosphatase is an important enzyme in glycerolipid biosynthesis, but difficult to purify. A purified preparation of N-ethylmaleimide-sensitive phosphatidate phosphatase from the yeast Saccharomyces cerevisiae was obtained by a five-step protocol, using chromatography on DE-53/DEAE FF, Affi-Gel Blue, hydroxyapatite, Mono-Q, and Superdex 200. A protease-deflcient yeast strain gave preparations similar to those of the wild-type strain. In exclusion chromatography, the enzyme activity of all preparations eluted at approximately the same position as albumin. However, the behavior on SDS/PAGE differed considerably among preparations, suggesting a multimeric subunit structure or degradation during purification. A 35-kDa and a 40-kDa protein band which coincided with activity were found in all preparations. Glycerol in the buffers could be excluded without rapid loss of enzyme activity, and Tris could be substituted for ammonium bicarbonate, while at least 0.6% sodium cholate in the buffers was essential.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022501212045
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  • 2
    Electronic Resource
    Electronic Resource
    Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato (1994)
    Springer
    Plant molecular biology 26 (1994), S. 327-338 
    Details
    ISSN: 1573-5028
    Keywords: Solanum tuberosum ; yeast ; polyamines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract S-adenosylmethionine decarboxylase (SAMDC) is involved in the biosynthesis of the polyamines, spermidine and spermine. Recently, we reported the isolation of a putative cDNA clone of the SAMDC clone of potato (Plant Mol Biol 20; 641–651). In order to confirm that the potato genes does encode SAMDC, a complementation experiment with a yeast strain that possesses a null mutation in the SAMDC gene was performed. The yeast strain contains a deletion-insertion mutation in the SAMDC gene and has an absolute requirement for the addition of exogenous spermidine for growth. When the full-length potato cDNA was expressed in the mutant yeast strain there was no longer a requirement for exogenous spermidine. Immunoblotting experiments suggest that the potato SAMDC gene product has an apparent molecular mass of 39 kDa. Expression of the SAMDC gene was high in the young and actively dividing tissues and low in the mature and non-dividing tissues of both vegetative and reproductive organs. Additionally, isolation and characterisation of the corresponding genomic clone is reported. The gene has one intron in its 5′-untranslated sequence but otherwise the transcribed portion is identical to the cDNA clone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00039543
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  • 3
    Electronic Resource
    Electronic Resource
    Yeast Protein Serine/Threonine Phosphatases: Multiple Roles and Diverse Regulation (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1647-1675 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; phosphorylation ; protein phosphatase ; PP1 ; PP2A ; PP2B ; calcineurin ; Sit4 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Since the isolation of the first yeast protein phosphatase genes in 1989, much progress has been made in understanding this important group of proteins. Yeast contain genes encoding all the major types of protein phosphatase found in higher eukaryotes and the ability to use powerful genetic approaches will complement the wealth of biochemical information available from other systems. This review will summarize recent progress in understanding the structure, function and regulation of the PPP family of protein serine-threonine phosphatases, concentrating on the budding yeast Saccharomyces cerevisiae.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Cloning and analysis of the Kluyveromyces lactis TRP1 gene: A chromosomal locus flanked by genes encoding inorganic pyrophosphatase and histone H3 (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 5 (1989), S. 35-50 
    Details
    ISSN: 0749-503X
    Keywords: TRP1 ; histone H3 ; histone H4 ; pyrophosphatase ; Kluyveromyces ; yeast ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The TRP1 gene of the yeast Kluyveromyces lactis has been cloned from a genomic library by complementation of the Saccharomyces cerevisiae trpl-289 mutation. The gene was located within the clone by transposon mutagenesis and the coding region identified by DNA sequencing. This has indicated that K. lactis TRP1 encodes a 210-amino acid polypeptide which shows 53% identity to the homologous S. cerevisiae protein. The K. lactis TRP1 gene has been disrupted by substituting the S. cerevisiae URA3 gene for a large part of the TRP1 coding sequence. Replacement of the chromosomal TRP1 locus with this construction has enabled the production of non-reverting trp1- strains of K. lactis, while a genetic analysis of the disrupted allele confirmed that the TRP1 gene had been cloned. DNA sequencing has also shown that the K. lactis TRP1 sequences is flanked by genes encoding inorganic pyrophosphatase and histone H3, which we have designated IPP and HHT1 respectively. Hybridization studies have shown that in common with S. cerevisiae, K. lactis has two copies of the histone H3 gene. Each H3 gene is closely linked to a gene encoding histone H4 and in both yeast species the IPP gene is tightly linked to one of the histone gene pairs.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320050106
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