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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Plant pathology 40 (1991), S. 0 
    ISSN: 1365-3059
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Amongst 489 mass isolates of Botrytis cinerea obtained from protected crops in Humberside during 1989, 67.3% were resistant to benomyl and 45.6% to vinclozolin. Two isolates resistant to dichlofluanid were obtained with EC50 values for mycelial growth on agar of 21.45 and 19.78 μg dichlofluanid/ml, respectively, compared with values of 1.55-2.56 μg/ml for sensitive isolates. EC50 values for germ tube emergence and length were much lower than for mycelial growth. In population studies carried out on tomatoes in a polythene tunnel, resistance to dichlofluanid and to vinclozolin declined over a 12-week period in the absence of fungicides. Field isolates of B. cinerea resistant to dichlofluanid were also resistant to vinclozolin. but strains resistant to dichlofluanid and sensitive to vinclozolin were obtained during population studies. Examination of a number of features of dichlofluanid-resistant strains revealed a degree of lack of fitness as compared with sensitive strains. There is no indication that resistance to dichlofluanid poses a great threat to the control of grey mould in Humberside at present.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 18 (1990), S. 65-70 
    ISSN: 1432-0983
    Keywords: Aspergillus nidulans ; ADHII
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary There are at least three alcohol dehydrogenases in Aspergillus nidulans. ADHII has been observed in polyacrylamide gels stained for ADH activity but, unlike ADHI and ADHIII, no physiological function has been attributed to it. This paper describes mutations that have been isolated from strains carrying a deletion in the structural gene for ADHI (alcA) and its adjacent positively-acting regulatory gene (alcR) that restore some ability to utilise ethanol as a carbon source. The mutations map at three loci, and all show elevated levels of the ADHII staining band. An assay for ADHII has been developed. The growth on ethanol has been shown to be dependent on the previously identified aldehyde dehydrogenase (structural gene, aldA). Two of the mutations, alcD and alcE, represent newly discovered mutations affecting ethanol utilisation while the third mutation is in amdA, a previously described trans-acting regulatory protein.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 12 (1987), S. 141-148 
    ISSN: 1432-0983
    Keywords: Informational suppressors ; Aspergillus nidulans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Seven allele specific gene unspecific suppressors mapping at four loci have been described previously (Roberts et al. 1979). Three new suppressors mapping in suaA are characterised, and the spectrum of suppression of all the suppressors with respect to seventeen suppressible mutations in eight different genes is described. Two distinct classes of suppressor are defined. The diversity of suppression of five suaA alleles, and the temperature sensitivity of some suaA suppressor mutant combinations but not others, suggests that suppressors at this locus are acting via ribosomal protein alteration. suaC109, a mutation that results in cold-sensitivity for growth shows a similar broad spectrum of suppression. Suppressors at the suaA and suaC loci suppress mutations that have the properties of chain termination mutations as well as missense mutations. suaB111, and suaD103 and suaD108 have a very restricted range of suppression. These suppressors may be mutations in tRNA genes.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0983
    Keywords: Key words  Alcohol dehydrogenase II ; Aspergillus nidulans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract   Alcohol dehydrogenase II (ADH II, structural gene alcB) was purified from a strain H1035, biA1; alcE1; alc500 alcD1, which produces 100-times more ADH II activity than the alcAalcR deletion strain (alc500). Antibodies were raised against this ADH, and were used to screen a cDNA library in λgt11. We have isolated the gene for an ADH which is over-expressed in H1035, and which we believe to be the alcB gene; cDNA and genomic clones were sequenced. The sequence contains three introns and encodes a protein of 367 amino acids. This protein shows a clear level of identity to a range of alcohol dehydrogenases, but is no more closely related to the ADH I and ADH III previously described in A. nidulans than to the ADHs of S. pombe and S. cerevisiae. The significance of consensus sequences found in the 5′ region of the gene is discussed in relation to the regulation of the gene.
    Type of Medium: Electronic Resource
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