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  • 1
    Electronic Resource
    Electronic Resource
    Cloning of the Rhizopus niveus pyr4 gene and its use for the transformation of Rhizopus delemar (1995)
    Springer
    Current genetics 27 (1995), S. 472-478 
    Details
    ISSN: 1432-0983
    Keywords: Rhizopus niveus ; pyr4 ; Rhizopus delemar ; Transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have cloned a pyr4 gene encoding orotidine-5′-monophosphate decarboxylase of the filamentous fungus Rhizopus niveus. The pyr4 gene of R. nivens has an open reading frame composed of 265 amino-acid residues and has two putative introns. We have also isolated a pyr4 mutant of Rhizopus delemar from 5-fluoroorotic acid-resistant mutants and transformed it with the pyr4 gene of R. niveus as a selectable marker. Introduced DNA was integrated into the chromosome in a multiple tandem array. The mitotic stability of the introduced DNA was increased by a repeated sporulation process. The expression of the Escherichia coli β-glucuronidase gene in R. delemar was successfully obtained under the control of the pgk2 gene promoter of R. niveus by co-transformation with the pyr4 gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00311218
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Nitric oxide reduction, the last step in denitrification by Fusarium oxysporum, is obligatorily mediated by cytochrome P450nor (2000)
    Springer
    Molecular genetics and genomics 263 (2000), S. 342-348 
    Details
    ISSN: 1617-4623
    Keywords: Key words Denitrification ; Cytochrome P450 ; Nitric oxide reductase ; Fusarium oxysporum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The involvement of cytochrome P450nor (P450nor) is the most striking feature of the fungal denitrifying system, and has never been shown in bacterial systems. To establish the physiological significance of the P450nor, we constructed and investigated mutants of Fusarium oxysporum that lacked the gene for P450nor. We mutated the gene by targeted integration of a disrupted gene into the chromosome of F. oxysporum. The mutants were shown to contain neither P450nor protein nor nitric oxide (NO) reductase (Nor) activity, implying that they are indeed deficient in P450nor. These mutants had apparently lost the denitrifying activity and failed to evolve nitrous oxide (N2O) upon incubation under oxygen-limiting conditions in the presence of nitrate. Their mycelia exhibited normal levels of dissimilatory nitrite reductase (Nir) activity and were able to evolve NO under these conditions. The promoter region of the P450nor gene was fused to lacZ and introduced into the wild-type strain of F. oxysporum. The transformed strain produced β-galactosidase under denitrifying conditions as efficiently as the wild type does P450nor. These results represent unequivocal genetic evidence that P450nor is essential for the reduction of NO to N2O, the last step in denitrification by F. oxysporum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380051177
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A fungal chitinase gene fromRhizopus oligosporus confers antifungal activity to transgenic tobacco (1997)
    Springer
    Plant cell reports 16 (1997), S. 439-443 
    Details
    ISSN: 1432-203X
    Keywords: Fungal chitinase ; Transgenic tobacco ; Antifungal activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have studied whether a chitinase involved in cell autolysis of a filamentous fungus,Rhizopus oligosporus, can operate as an antifungal defense system in tobacco. Thechi1 gene was introduced into tobacco by theAgrobacterium tumefaciens leaf disc system. Among 22 transgenic tobacco plants, 2 were selected and their individual homozygous progeny, Tch1-1 and Tch2-1, were studied. Chitinase activity in the extracts of young leaves from Tch1-1 or Tch2-1, in which thechi1 gene product was detected by Western blot analysis, was three- to four-fold higher than that from the control plants. A fungal infection assay on the leaves infected with the discomycete pathogensSclerotinia sclerotiorum andBotrytis cinerea revealed that the symptoms observed with these two were remarkably suppressed as compared with the control leaves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01092762
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    A fungal chitinase gene from Rhizopus oligosporus confers antifungal activity to transgenic tobacco (1997)
    Springer
    Plant cell reports 16 (1997), S. 439-443 
    Details
    ISSN: 1432-203X
    Keywords: Key words Fungal chitinase ; Transgenic tobacco ; Antifungal activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have studied whether a chitinase involved in cell autolysis of a filamentous fungus, Rhizopus oligosporus, can operate as an antifungal defense system in tobacco. The chi1 gene was introduced into tobacco by the Agrobacterium tumefaciens leaf disc system. Among 22 transgenic tobacco plants, 2 were selected and their individual homozygous progeny, Tch1-1 and Tch2-1, were studied. Chitinase activity in the extracts of young leaves from Tch1-1 or Tch2-1, in which the chi1 gene product was detected by Western blot analysis, was three- to four-fold higher than that from the control plants. A fungal infection assay on the leaves infected with the discomycete pathogens Sclerotinia sclerotiorum and Botrytis cinerea revealed that the symptoms observed with these two were remarkably suppressed as compared with the control leaves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01092762
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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