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  • Phenothiazine derivatives  (1)
  • σ 32  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Co-induction of DNA relaxation and synthesis of DnaK and GroEL proteins inEscherichia coli by expression of LetD (CcdB) protein, an inhibitor of DNA gyrase encoded by the F factor (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 593-600 
    Details
    ISSN: 1617-4623
    Keywords: DNA relaxation ; Heat shock response ; LetD (CcdB) protein ; DNA gyrase ; σ 32
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We examined the influence of overexpression of LetD (CcdB) protein, an inhibitor of DNA gyrase encoded by the F factor ofEscherichia coli, on DNA supercoiling and induction of heat shock proteins. Cells were transformed with a plasmid carrying the structural gene for LetD protein under control of thetac promoter, and LetD protein was induced by adding isopropylβ-d-thiogalactopyranoside (IPTG) to the culture medium. Analysis by agarose gel electrophoresis in the presence of chloroquine revealed relaxation of plasmid DNA in cells depending on the concentration of IPTG employed for induction. Protein pulse-labeling experiments with [35S]methionine and cysteine revealed that synthesis of DnaK and GroEL proteins was also induced by IPTG, and concentrations necessary for DNA relaxation and induction of the heat shock proteins were much the same. Expression of mutant LetD protein lacking two amino acid residues at the C-terminus induced neither DNA relaxation nor the synthesis of DnaK and GroEL proteins. Induction of wild-type LetD protein but not mutant LetD protein markedly enhanced synthesis ofσ 32. We interpret these results to mean that DNA relaxation in cells caused by the expression of LetD protein induces heat shock proteins via increased synthesis ofσ 32.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174447
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  • 2
    Electronic Resource
    Electronic Resource
    Phenotypes of dnaA mutants of Escherichia coli sensitive to phenothiazine derivatives (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 212-215 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsEscherichia coli ; Phenothiazine derivatives ; DnaA protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activation of DnaA protein by cardiolipin is inhibited by fluphenazine in vitro. We therefore examined the sensitivity of temperature-sensitive dnaA mutants of Escherichia coli to fluphenazine and other phenothiazine derivatives. Among the eight dnaA mutants tested, dnaA5, dnaA46 dnaA602, and dnaA604, mutants with mutations in the putative ATP binding site of DnaA protein, showed higher sensitivities to phenothiazine derivatives than did the wild-type strain. The dnaA508 and dnaA167 mutants, which have mutations in the N-terminal region of DnaA protein, also showed higher sensitivities to phenothiazine derivatives. On the other hand, the dnaA204 and dnaA205 mutants, with lesions in the C-terminal region of the DnaA protein, showed the same sensitivity to phenothiazine derivatives as the wild-type strain. Complementation analysis with a plasmid containing the wild-type dnaA gene and phage P1-mediated transduction confirmed that dnaA mutations are responsible for these sensitivity phenotypes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004389670024
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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