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  • Catabolite derepression  (1)
  • Key words. Nickel enzymes; nickel transport; nickel-processing proteins; metal chaperonin proteins; metallocluster assembly; urease; hydrogenase; CO-dehydrogenase.  (1)
  • Oxidative stress survival  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Nickel-binding proteins (1999)
    Springer
    Cellular and molecular life sciences 56 (1999), S. 604-625 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Nickel enzymes; nickel transport; nickel-processing proteins; metal chaperonin proteins; metallocluster assembly; urease; hydrogenase; CO-dehydrogenase.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Nickel enzymes are a relatively new class of metalloenzymes. The seven known nickel enzymes are urease, hydrogenase, CO-dehydrogenase, methyl-coenzyme M reductase, Ni-superoxide dismutase, glyoxalase I and cis-trans isomerase. The requirement for nickel implies the presence of a nickel-processing system, since free transition metals are harmful to the cell. A nickel-processing system involves the recognition and transport of nickel into the cell and the handling of the nickel once it enters the cell until it is inserted into the nickel enzyme. Several mechanisms for nickel transport have been identified and will be reviewed here. Accessory proteins required for the biosynthesis of the nickel active site have been identified. Accessory proteins bind the nickel when it enters the cell and are proposed to assist with the insertion of nickel into the enzyme. The function of the characterized nickel-processing proteins is described, and models for nickel insertion into the nickel enzymes are presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000180050456
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    UBI4, the polyubiquitin gene of Saccharomyces cerevisiae, is a heat shock gene that is also subject to catabolite derepression control (1997)
    Springer
    Molecular genetics and genomics 253 (1997), S. 439-447 
    Details
    ISSN: 1617-4623
    Keywords: Key words Saccharomyces cerevisiae ; Polyubiquitin gene ; Catabolite derepression ; Oxidative stress survival
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Carbon and nitrogen regulation of UBI4, the stress-inducible polyubiquitin gene of Saccharomyces cerevisiae, was investigated using a UBI4 promoter-LacZ fusion gene (UBI4-LacZ). Expression of this gene in cells grown on different media indicated that the UBI4 promoter is more active during growth on respiratory than on fermentable carbon sources but is not subject to appreciable control by nitrogen catabolite repression. UBI4-LacZ expression was virtually identical in cells having constitutively high (ras2, sra1-13) or constitutively low (ras2) levels of cyclic AMP-dependent protein kinase activity, indicating that this kinase does not exert a major influence on UBI4 expression. Catabolite derepression control of the UBI4 promoter was confirmed by measurements of UBI4-LacZ expression in hap mutant and wild-type strains before and after transfer from glucose to lactate. Mutagenesis of the perfect consensus for HAP2/3/4 complex binding at position −542 resulted in considerable reduction of UBI4 promoter derepression with respiratory adaptation in HAP wild-type cells and abolished the reduced UBI4-LacZ derepression normally seen when aerobic cultures of the hap1 mutant are transferred from glucose to lactate. This HAP2/3/4 binding site is therefore a major element contributing to catabolite derepression of the UBI4 promoter, although data obtained with hap1 mutant cells indicated that HAP1 also contributes to this derepression. The HAP2/3/4 and HAP1 systems are normally found to activate genes for mitochondrial (respiratory) functions. Their involvement in mediating higher activity of the UBI4 promoter during respiratory growth may reflect the contribution of UBI4 expression to tolerance of oxidative stress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050341
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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