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  • 1
    Electronic Resource
    Electronic Resource
    Expression of the Escherichia coli β-glucuronidase gene in industrial and phytopathogenic filamentous fungi (1989)
    Springer
    Current genetics 15 (1989), S. 177-180 
    Details
    ISSN: 1432-0983
    Keywords: Reporter gene ; Filamentous fungi ; Pathogenicity ; β-glucuronidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A chimaeric β-glucuronidase (GUS) gene has been created by ligating the Aspergillus nidulans glyceraldehyde 3-phosphate dehydrogenase promoter to the coding sequence of the E. coli uidA gene. Cotransformation of this vector into A. nidulans, A. niger and the tomato pathogen Fulvia fulva (syn. Cladosporium fulvum (Cooke)) resulted in the expression of β-glucuronidase. GUS activity was detected by growth on agar media containing X-gluc and by enzyme assays of mycelial extracts. Expression of the gene in F. fulva transformants was also easily detectable during growth in plants and did not affect pathogenicity. These results form the basis for a versatile and sensitive reporter gene system for industrial and phytopathogenic filamentous fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00435503
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A glycoprotein associated with the acquisition of the self-incompatibility system by maturing stigmas of Brassica oleracea (1979)
    Springer
    Planta 146 (1979), S. 179-183 
    Details
    ISSN: 1432-2048
    Keywords: Brassica ; Cellular recognition ; Glycoproteins ; Self-incompatibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Iso-electric focusing of extracts derived from stigmatic homogenates of Brassica oleracea reveals that the mature stigma possesses large quantities of a glycoprotein not present in earlier stages of development in the bud. Pollen germination experiments carried out in parallel with the biochemical tests suggest that the appearance of this glycoprotein, which has an isoelectric point of pH 5.8, is coincident with the development of the self-incompatibility response. The site of this protein, and the role it may play in pollen-stigma interactions are discussed in terms of current models of the self-incompatibility system in Brassica.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388229
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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