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  • 1
    Electronic Resource
    Electronic Resource
    Disruption of the cyclosporin synthetase gene of Tolypocladium niveum (1994)
    Springer
    Current genetics 26 (1994), S. 461-467 
    Details
    ISSN: 1432-0983
    Keywords: Cyclosporin ; Non-ribosomal peptide synthesis ; Tolypocladium niveum ; Transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cyclosporin A is a potent and clinically-important immunosuppressive drug (SandimmunR). It is produced by the fungus Tolypocladium niveum. A transformation system for T. niveum ATCC34921 based on hygromycin selection was established. In order to obtain a T. niveum promoter, the cyclophilin gene was isolated using the Neurospora crassa gene as probe. A plasmid vector was constructed in which the promoter region of the T. niveum cyclophilin gene was fused to a bacterial hygromycin phosphotransferase gene. Protoplasts were transformed with this plasmid and hygromycin-resistant transformants were isolated. Using this transformation system, mutants of T. niveum with disrupted versions of the cyclosporin synthetase gene (simA) were engineered by DNA-mediated transformation. Disruption of the gene resulted in loss of the ability to produce cyclosporins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309935
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame (1994)
    Springer
    Current genetics 26 (1994), S. 120-125 
    Details
    ISSN: 1432-0983
    Keywords: Domain structure ; N-methyltransferase ; Non-ribosomal peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cyclosporin A, a potent and clinically-important immunosuppressive drug (SandimmunR), is synthesized from its precursor amino acids by cyclosporin synthetase, a single multi-functional enzyme. In this study we report the cloning of the corresponding coding region of this synthetase. It contains an open reading frame of 45.8 kb which encodes a peptide with a calculated Mr of 1 689 243. The predicted gene product contains 11 aminoacid-activating domains that are very similar to one another and to the domains of other peptide synthetases. Seven of these domains harbour N-methyltransferase functions. This is the largest genomic ORF described so far.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00313798
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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