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  • 1
    Electronic Resource
    Electronic Resource
    Two nuclearly inherited loci conferring increased diuron resistance to NADH oxidase in Saccharomyces cerevisiae (1989)
    Springer
    Current genetics 15 (1989), S. 31-38 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Diuron ; Respiration ; Nuclear genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In Saccharomyces cerevisiae, diuron blocks the respiration pathway at the level of the bc1 complex. Nuclear diuron-resistant mutations which confer in vitro resistance to mitochondrial NADH oxidase have been identified. Five mutations were found to be clustered at two distinct nuclear loci, DIU3 and DIU4. The distance between the two loci was estimated to be about 36.7 cM. These loci do not appear to be centromere-linked and did not show a linkage to any of the genes coding for bc1 complex subunits. DIU3 and DIU4 loci might, therefore, code for other components of the respiratory chain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00445749
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  • 2
    Electronic Resource
    Electronic Resource
    Increased diuron resistance in the joint expression of mutations located at the DIU2, DIU3 and DIU4 loci of Saccharomyces cerevisiae (1989)
    Springer
    Current genetics 15 (1989), S. 121-127 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; Diuron ; Nuclear, mitochondrial mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In Saccharomyces cerevisiae, diuron blocks the respiratory pathway at the level of the bc1 complex. Two mitochondrially inherited loci, DIU1 and DIU2, located in the cytochrome b gene, and two nuclearly inherited loci, DIU3 and DIU4, have previously been identified. The present work genetically characterizes two double mutants. One mutant, Diu-217, carries two nuclearly inherited mutations, diu3-217a and diu-217b; the second mutant, Diu-783, carries the previously described nuclear mutation diu3-783 and a mitochondrial mutation diu2-783. Each mutation, independent of its location, exhibits a weak diuron resistance. The joint expression of two or three mutations leads to a cumulative or a cooperative enhanced diuron-resistant phenotype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00435458
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  • 3
    Electronic Resource
    Electronic Resource
    Sequence analysis of three deficient mutants of cytochrome oxidase subunit I of Saccharomyces cerevisiae and their revertants (1994)
    Springer
    Current genetics 26 (1994), S. 546-552 
    Details
    ISSN: 1432-0983
    Keywords: Cytochrome oxidase ; Revertant ; Mitochondria ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three respiratory-deficient mutants of cytochrome oxidase subunit I in the yeast mitochondrion have been sequenced. They are located in, or near, transmembrane segment VI, the catalytic core of the enzyme. Respiratory-competent revertants have been selected and studied. The mutant V244M was found to revert at the same site in valine (wild-type), isoleucine or threonine. The revertants of the mutant G251R were of three types: glycine (wild-type), serine and threonine at position 251. A search for second-site mutations was carried out but none were found. Among 60 revertants tested, the mutant K265M was found to revert only to the wild-type allele.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309948
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  • 4
    Electronic Resource
    Electronic Resource
    Fructose-bisphosphatase-deficient mutants of the yeast Schizosaccharomyces pombe (1982)
    Springer
    Archives of microbiology 133 (1982), S. 131-136 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00413526
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  • 5
    Electronic Resource
    Electronic Resource
    A cytoplasmic gene for partial suppression of a nuclear pleiotropic respiratory deficient mutant in the petite negative yeast Schizosaccharomyces pombe (1976)
    Springer
    Molecular genetics and genomics 149 (1976), S. 101-109 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nuclear pleiotropic respiratory-deficient mutant pet1 (previously M126) exhibits cytochromes aa3 and b deficiencies accompanied by loss of the oligomycin-sensitivity of the mitochondrial ATPase. The mutant pet1, unable to grow on glycerol, exhibits in addition sensitivity of Antimycin A of the growth on glucose. The latter phenotypic trait symbolized by ANAS-D, exhibits a high frequency (2 to 4×10-5) of spontaneous suppression into Antimycin A-resistant strains. Mutagenesis with MnCl2 increases by a factor of 102 the frequency of ANAR-D derivatives. This suppression is partial since none of the suppressed strains is able to grow on glycerol even when respiratory functions and cytochromes activities are restored as in the pet1 [SUP2] strain. In the latter strain it is concluded that the extralocus suppressor gene [SUP2] is responsible for the ANAR-D trait. Tetrad analysis in a cross homozygous for pet1 demonstrates a non-Mendelian segregation pattern for the SUP2 suppressor gene. In stable diploids, homozygous for pet1, the [SUP2] suppressor exhibits a mitotic segregation pattern. Furthermore the transmission of the [SUP2] gene is decreased by ethidium bromide treatment. Therefore, the [SUP2] suppressor gene responsible for partial suppression of the nuclear pleiotropic phenotype in mutant pet1 is of cytoplasmic heredity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00275964
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  • 6
    Electronic Resource
    Electronic Resource
    Basic for slow growth on non-fermentable substrates by a Saccharomyces cerevisiae mutant UV-sensitive for rho− production (1978)
    Springer
    Molecular genetics and genomics 164 (1978), S. 227-234 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mutant uvsρ 72 of Saccharomyces cerevisiae UV-sensitive for rho- production displays slower growth on media containing non-fermentable carbon sources such as glycerol or lactate. The slower growth on glycerol is not due to any deficiency in glycerol catabolism or mitochondrial oxidative phosphorylation. No modifications of the sensitivity to ethidium bromide of the mitochondrial ATPase activity could be detected. A mathematical model is presented which accounts for slower growth of uvsρ 72 on the sole basis of the continuous and elevated rho- production in the mutant strain. This model, which estimates the rate of mutation from the rate of growth and vice versa, has been verified experimentally in the case of uvsρ 72. The model has been generalised, so that it can be used for any microbial population subject to constant and high rates of any type of mutation providing that the mutant is stable, and either unable to grow or able to grow at this own rate different from that of the parental strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267388
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  • 7
    Electronic Resource
    Electronic Resource
    Nucleo-cytoplasmic interaction between oligomycin-resistant mutations in Saccharomyces cerevisiae (1974)
    Springer
    Molecular genetics and genomics 135 (1974), S. 309-326 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. A single-gene nuclear mutant of Saccharomyces cerevisiae, isolated as oligomycin-resistant, exhibits in vivo cross-resistance to venturicidin and collateral sensitivity to Synthalin. All three compounds are inhibitors of mitochondrial oxidative phosphorylation. Oligomycin resistance and Synthalin sensitivity are recessive, while venturicidin resistance is dominant. 2. A cytoplasmic mutant, also isolated as oligomycin-resistant, shows collateral sensitivity to both Synthalin and venturicidin. All three traits undergo mitotic segregation in diploids formed by crossing mutant and normal haploids. 3. A novel nucleocytoplasmic interaction is observed in diploids formed by crossing haploid strains containing the nuclear and the cytoplasmic mutations, respectively. The dominant venturicidin resistance determined by the nuclear gene undergoes mitotic segregation, which results from a suppression of the nuclear phenotype by the cytoplasmic mutation. When a diploid mitotic segregant contains primarily mutant-type mitochondria, venturicidin resistance is completely suppressed. In haploids containing both the nuclear and cytoplasmic mutations, suppression is only partial. 4. Oxidative phosphorylation and ATPase in mitochondrial fractions isolated from cytoplasmic mutant cells are less sensitive to inhibition by oligomycin than normal, but in vitro sensitivity to venturicidin is not significantly changed. In similar mitochondrial fractions isolated from normal and nuclear mutant cells, no significant differences in sensitivity to either inhibitor are detected. 5. The molecular basis for the nucleocytoplasmic suppression of venturicidin resistance may involve participation of mitochondrial membrane, plasma membrane or both. Either mitochondria can undergo changes in venturicidin sensitivity upon isolation, or the molecular entity which controls access of venturicidin to the mitochondria resides outside of the organelles. 6. Our data establish that aspects of the response in vivo of both venturicidin and Synthalin are controlled by the mitochondrial genome. 7. The nucleocytoplasmic interaction described here is the first example in which a specific restricted mitochondrial mutation modifies the phenotypic expression of a nuclear gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271146
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  • 8
    Electronic Resource
    Electronic Resource
    Genetic localization of diuron- and mucidin-resistant mutants relative to a group of loci of the mitochondrial DNA controlling coenzyme QH2-cytochrome c reductase in Saccharomyces cerevisiae (1979)
    Springer
    Molecular genetics and genomics 167 (1979), S. 287-298 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Diuron-resistance, DIU (Colson et al., 1977), antimycin-resistance, ANA (Michaelis, 1976; Burger et al., 1976), funiculosin-resistance, FUN (Pratje and Michaelis, 1977; Burger et al., 1977) and mucidin-resistance, MUC (Subik et al., 1977) are each coded by a pair of genetic loci on the mit DNA of S. cerevisiae. In the present paper, these respiratory-competent, drug-resistant loci are localized relative to respiratory-deficient BOX mutants deficient in coenzyme QH2-cytochrome c reductase (Kotylak and Slonimski, 1976, 1977) using deletion and recombination mapping. Three drug-resistant loci possessing distinct mutated allelic forms are distinguished. DIU1 is allelic or closely linked to ANA2, FUN1 and BOX1; DIU2 is allelic or closely linked to ANA1, MUC1 and BOX4/5; MUC2 is allelic to BOX6. The high recombinant frequencies observed between the three loci (13% on the average for 33 various combinations analyzed) suggest the existence of either three genes coding for three distinct polypeptides or of a single gene coding for a single polypeptide but subdivided into three easily separable segments. The resistance of the respiratory-chain observed in vitro in the drug-resistant mutants and the allelism relationships between respiratory-competent, drug-resistant loci and coQH2-cyt c reductase deficient, BOX, loci strongly suggest that each of the three drug-resistant loci codes for a structural gene-product which is essential for the normal coQH2-cyt c reductase activity and is obviously a good candidate for a gene product of the drug-resistant loci mapped in this paper. Polypeptide length modifications of cytochrome b were observed in mutants deficient in the coQH2-cyt c red and localized at the BOX1, BOX4 and BOX6 genetic loci (Claisse et al., 1977, 1978) which are precisely the loci allelic to drug resistant mutants as shown in the present work. Taken together these two sets of data provide a strong evidence in favor of the idea that there exist three non contiguous segments of the mitochondrial DNA sequence which code for a single polypeptide sequence of cytochrome b. In each segment mutations which modify the polypeptide sequence can occur leading to the loss (BOX mutants) or to a modification (drug resistant mutants) of the enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267421
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  • 9
    Electronic Resource
    Electronic Resource
    Random mutant generation and its utility in uncovering structural and functional features of cytochromeb inSaccharomyces cerevisiae (1993)
    Springer
    Journal of bioenergetics and biomembranes 25 (1993), S. 211-220 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00762583
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  • 10
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    Fructose-bisphosphatase-deficient mutants of the yeast Schizosaccharomyces pombe (1982)
    Springer
    Details
    Publication Date: 1982-01-01
    Print ISSN: 0302-8933
    Electronic ISSN: 1432-072X
    Topics: Biology
    Published by Springer
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