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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 250 (1996), S. 169-179 
    ISSN: 1617-4623
    Keywords: Key words Alcaligenes eutrophus ; pMOL28 ; Plasmid replication ; Plasmid partition ; Plasmid stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A 4.64 kb region of the 180 kb heavy metal resistance plasmid pMOL28 of Alcaligenes eutrophus CH34, previously shown to be able to replicate autonomously, was sequenced and analyzed. Three genes involved in plasmid maintenance were identified: parA28 and parB28 are involved in plasmid partitioning and stability, while repA28 encodes a protein required for replication. In addition to the parAB28 genes, a third locus, parS28, required in cis for active partitioning was identified. The parABS28 locus of pMOL28 shows strong similarity in organization to the sop, par and rep regions, respectively, of the Escherichia coli F-factor, the E. coli P1 and P7 prophages, and the Agrobacterium pTiB6S3 and pRiA4b plasmids. The ParAB28 proteins of pMOL28 also show similarity to the proteins encoded by two conserved open reading frames present in the replication regions of the Pseudomonas putida and Bacillus subtilus chromosomes. The functionality of the pMOL28 par region was examined by performing stability and incompatibility tests between pMOL28 and pMOL846 or pMOL850, which contain the 4.64 EcoRI replicon fragment of pMOL28, cloned in opposite orientations into pSUP202, which is itself unable to replicate in A. eutrophus. The RepA28 replication protein showed similarity to the RepL protein of P1, which is required for lytic replication of this E. coli phage. The replication origin of pMOL28, oriV28, seems to be located within the repA28 coding region, and pMOL28 replication may depend on transcriptional activation of oriV28.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 20 (1998), S. 61-68 
    ISSN: 1476-5535
    Keywords: Keywords: siderophore; Alcaligenes eutrophus; heavy metal resistance; czc; bioavailability; biosensor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Alcaligin E, the siderophore of the heavy metal-resistant A. eutrophus strain CH34, was shown to interact with Cd and consequently affect its bioavailability and toxicity. The addition of alcaligin E markedly stimulated the growth in the presence of Cd of an alcaligin E-deficient CH34 derivative. Using bioluminescence assays, this effect could be assigned to a decrease in bioavailability of Cd in the presence of alcaligin E. However, Cd-uptake studies showed no influence of alcaligin E on the cellular concentration of Cd. Furthermore, by scanning electron microscopy, the morphology of precipitated Cd crystals was shown to be altered by alcaligin E. These data suggest that alcaligin E, besides its function in iron supply to the cell, provides a protection against heavy metal toxicity. A link between the A. eutrophus CH34 siderophore system and the czc-mediated Cd-efflux system is hypothesized.
    Type of Medium: Electronic Resource
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