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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 154 (1977), S. 61-66 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The fdp mutation has been localized on the genome of Saccharomyces carlsbergensis, on chromosome II, between lys2 and tyr1, at a map distance of 31 centimorgan from lys2. Since the fdp mutant does not grow on glucose, fructose, mannose and sucrose, hexose transport and a number of enzymes of carbon metabolism were tested, but no significant differences could be found between the wild type and the mutant. Only the regulatory properties of glycogen synthetase are changed in the mutant, but it is doubtfull whether this can explain its phenotype. The disorganization of carbon metabolism of the mutant upon addition of glucose to the medium was analyzed in more detail. The most prominent feature observed until now is the accumulation of free glucose and hexose phosphates in the cell. This result indicates that somehow the feedback control between hexose transport and metabolism is impaired. Hexose phosphates are known to be toxic to many cells, including yeast. Therefore, accumulation of hexose phosphates in the presence of glucose in the medium, can explain the absence of growth on this carbon source.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 123 (1973), S. 233-246 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. In S. carlsbergensis 25 recessive mal 6-mutants were isolated, which did not complement each other in any combination. Maltose induces maltase and a maltose transport system in the wild type but not in the mutants. The derepression, however, of these activities on galactose is the same for the wild type and the mutants. We could not detect significant differences between some kinetic properties of partially purified maltase from the wild type and from one of the mutants (mal 6-13). 2. From mutant mal 6-6 (ϱ−) a number of temperature sensitive revertants was obtained, which grew on maltose at 26°, but not at 36°. Diploids made by crossing these temperature sensitive revertants with the mal 6-mutants (ϱ+) either did not grow on maltose at the restrictive temperature, or only weakly, and therefore the ts-revertants were considered to be mal 6-alleles. A biochemical study of some of the mal 6-ts-mutants indicated that the temperature sensitivity could not be explained by an inactivation or breakdown of maltase or of the maltose transport system at the restrictive temperature. From these results we concluded that the mal 6-ts-alleles and, consequently, all mal 6-alleles are alleles of a regulator gene rather than of a structural gene for maltase or maltose permease. 3. Maltose negative segregants from crosses between strains, carrying one of the polymeric genes MAL 3, MAL 4 or MAL 6, were shown to contain a basal activity of maltase and of maltose transport. Partially purified maltase from two of those mal-segregants had comparable properties to wild type maltase (MAL 6), indicating the presence of maltase cistrons in the parent strains, not linked to the MAL-gene. 4. Indications that the mal 6-mutants are regulatory mutants in a positive regulation system are discussed as well as possible explanations for the fact that no structural mutants for maltase could be detected.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 125 (1973), S. 139-146 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. The isolation in S. carlsbergensis of a mutant (C 2), constitutive for maltase and for maltose transport is described. This mutant, in crosses behaving as closely linked or allelic to MAL 6, is different from the constitutive MAL 4-mutant, described by other authors, in four respects: C 2 is recessive to the wild type; the mutant is sensitive to catabolite repression; the level of maltase is not superinducible by maltose; and maltase produced in response to C 2 is not different from wild type maltase. 2. Hybrids made by crossing C 2 with a number of mal 6-mutants grow on maltose and maltase is induced by maltose as in the wild type MAL 6-strain. 3. The properties of C 2 are discussed and compared with litterature data on positive enzyme regulation.
    Type of Medium: Electronic Resource
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