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  • 1995-1999  (3)
  • Actinomycetes  (2)
  • ATP-binding protein  (1)
  • Recombinant DNA
  • 1
    Electronic Resource
    Electronic Resource
    An ABC transporter is essential for resistance to the antitumor agent mithramycin in the producerStreptomyces argillaceus (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 692-698 
    Details
    ISSN: 1617-4623
    Keywords: Streptomyces ; ABC transporters ; ATP-binding protein ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mithramycin is an antitumor antibiotic synthesized byStreptomyces argillaceus. This producer strain is highly resistant in vivo to mithramycin (MIC 100 µg/ml) but sensitive to the related drugs chromomycin and olivomycin (MIC 10 µg/ml). From a genomic library ofS. argillaceus DNA two cosmid clones were isolated which confer a high level of resistance to mithramycin onS. albus. The resistance genes were mapped by subcloning to a 3.9-kbPstI-PvuII fragment. DNA sequence analysis of this fragment revealed one incomplete and three complete open reading frames. Subcloning experiments demonstrated that resistance to mithramycin is mediated by the genesmtrA andmtrB. ThemtrA gene can potentially encode an ATP-binding protein of the ABC transporter superfamily, containing one nucleotide-binding domain and showing similarity with other ABC transporters involved in resistance to daunorubicin, oleandomycin and tetronasin in their respective producer strains. ThemtrB gene codes for an integral membrane protein with six putative transmembrane helices. A mithramycin-sensitive mutant was generated in a gene replacement experiment by disrupting themtrA gene, thus demonstrating that the system encoded by themtrAB genes is essential for conferring resistance to mithramycin inS. argillaceus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174118
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Analysis of a Streptomyces antibioticus chromosomal region involved in oleandomycin biosynthesis, which encodes two glycosyltransferases responsible for glycosylation of the macrolactone ring (1998)
    Springer
    Molecular genetics and genomics 259 (1998), S. 299-308 
    Details
    ISSN: 1617-4623
    Keywords: Key words Macrolides ; Glycosyltransferase ; Deoxyhexoses ; Actinomycetes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 6-kb region from the chromosome of Streptomyces antibioticus, an oleandomycin producer, was cloned and sequenced. This region was located between the 3′ end of the gene encoding the third subunit of the oleandomycin type I polyketide synthase and the oleP and oleB genes, which encode a cytochrome P450 monooxygenase and an oleandomycin resistance gene, respectively. Analysis of the nucleotide sequence revealed the presence of five genes encoding a cytochrome P450-like protein (oleP1), two glycosyltransferases (oleG1 and oleG2) involved in the transfer of the two 6-deoxysugars (L-oleandrose and D-desosamine) to the oleandomycin macrolactone ring, a methyltransferase (oleM1), and a gene (oleY) of unknown function. Insertional inactivation of this region by gene disruption generated an oleandomycin non-producing mutant which accumulated a compound that, according to mass spectrometry analysis, could correspond to the oleandomycin macrolactone ring (oleandolide), suggesting that the mutation affects oleandrosyl glycosyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050816
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Cloning, sequencing and transcriptional analysis of a Streptomyces coelicolor operon containing the rplM and rpsI genes encoding ribosomal proteins ScoL13 and ScoS9 (1997)
    Springer
    Molecular genetics and genomics 257 (1997), S. 91-96 
    Details
    ISSN: 1617-4623
    Keywords: Key words Ribosomal proteins S9/L13 ; Genes rpsI/rplM ; Actinomycetes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The N-terminal amino acid sequences of two peptides derived from a Streptomyces coelicolor ribosomal protein were determined and degenerate oligonucleotide primers derived from these sequences were used as probes for the screening of a chromosomal DNA library of S. coelicolor. Two positive clones were isolated and DNA sequencing of a 1740-bp region of these clones that hybridised with the probes revealed the presence of four genes, two of them incomplete. The deduced products of the two complete genes, rplM and rpsI, showed clear similarities to L13 and S9 ribosomal proteins from various organisms. Promoter-probe and primer extension experiments suggest that the two genes form a single transcriptional unit. The specific rate of synthesis of both proteins was high at early stages of growth but decreased later.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050627
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    Paper (German National Licenses)
    Fulltext
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