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  • Multiple activities  (1)
  • Oxytetracycline resistance  (1)
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Keywords
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  • 1
    Electronic Resource
    Electronic Resource
    Molecular cloning of resistance genes and architecture of a linked gene cluster involved in biosynthesis of oxytetracycline by Streptomyces rimosus (1989)
    Springer
    Molecular genetics and genomics 215 (1989), S. 231-238 
    Details
    ISSN: 1617-4623
    Keywords: Streptomyces rimosus ; Antibiotic production ; Oxytetracycline biosynthetic gene cluster ; Oxytetracycline resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The isolation of mutants of Streptomyces rimosus which were blocked in oxytetracycline (OTC) production was described previously. The genes for the early steps of antibiotic biosynthesis mapped together. Genomic DNA fragments of S. rimosus which conferred resistance to OTC and complemented all of these non-producing mutants have been cloned. The cloned DNA is physically linked within approximately 30 kb of the genome of S. rimosus. The gene cluster is flanked at each end by a resistance gene each of which, independently, can confer resistance to the antibiotic. In OTC-sensitive strains of S. rimosus, the entire gene cluster including both resistance genes has been deleted. Complementation of blocked mutants by cloned DNA fragments in multi-copy vectors was often masked by a secondary effect of switching off antibiotic productions in strains othersise competent to produce OTC. This adverse effect on OTC production was not observed with recombinants using low copy-number vectors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00339722
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Intracellular aminopeptidases inStreptomyces lividans 66 (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 24-29 
    Details
    ISSN: 1476-5535
    Keywords: Streptomyces lividans ; Aminopeptidases ; Intracellular ; Multiple activities
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary We have investigated the aminopeptidase activities present inStreptomyces lividans strains. The majority of these activities proved to be intracellular with multiple active species. Two aminopeptidase P genes were identified to be responsible for the ability to hydrolyze amino terminal peptide bonds adjacent to proline residues. Two other broad spectrum aminopeptidases were found to display homology at both the DNA and protein levels. One showed significant homology to PepN proteins, particularly around the putative zinc-binding residues which are important for catalysis. The second broad spectrum activity was not analyzed in detail but showed a different spectrum of substrate specificity to that of PepN.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569658
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    Paper (German National Licenses)
    Fulltext
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