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  • Fructose-bisphosphatase deficient mutants  (1)
  • resistance mutants  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 133 (1982), S. 131-136 
    ISSN: 1432-072X
    Keywords: Fructose-bisphosphatase deficient mutants ; Yeast ; Schizosaccharomyces pombe ; Gluconeogenesis ; Glucose repression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We showed that in the yeast Schizosaccharomyces pombe, fructose-bisphosphatase is not subject to catabolite inactivation as it was observed in Saccharomyces cerevisiae. However, this enzyme activity is sensitive to catabolite repression in both yeasts. Two mutants lacking completely fructose-bisphosphatase activity were found. They were unable to grow on glycerol medium. They were still respiratory competent and exhibited the ability to derepress partially malate dehydrogenase activity. In glucose exponential phase culture, the parental strain lacks completely the fructosebisphosphatase activity due to catabolite repression. In these conditions, the growth is slowed down only in the mutants eventhough both mutants and their parental strain lack this enzyme activity. Normal sporulation and poor spore germination were observed for one mutant whereas, only in the presence of glucose, normal sporulation and normal spore germination were observed for the second mutant. Mendelian segregation of glycerol growth was found for the well germinating mutant. It is of nuclear heredity. The two mutations appeared to be closely linked.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 25 (1993), S. 211-220 
    ISSN: 1573-6881
    Keywords: Cytochromeb structure and function ; random mutants ; yeast ; resistance mutants ; revertants of deficient mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The generation of random mutations in the mitochondrial cytochromeb gene ofSaccharomyces cerevisiae has been used as a most fruitful means of identifying subregions that play a key role in thebc 1 complex mechanism, best explained by the protonmotive Q cycle originally proposed by Peter Mitchell. Selection for center i and center o inhibitor resistance mutants, in particular, has yielded much information. The combined approaches of genetics and structural predictions have led to a two-dimensional folding model for cytochromeb that is most compatible with current knowledge of the protonmotive Q cycle. A three-dimensional model is emerging from studies of distant reversions of deficient mutants. Finally, interactions between cytochromeb and the other subunits of thebc 1 complex, such as the iron-sulfur protein, can be affected by a single amino acid change.
    Type of Medium: Electronic Resource
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