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  • 1
    Electronic Resource
    Electronic Resource
    Temperature shift-up leads to simultaneous and continuous plasmid DNA relaxation and induction of DnaK and GroEL proteins in anaerobically growing Escherichia coli cells (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 121 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract We previously reported that plasmid DNA in Escherichia coli cells growing under aerobic conditions relaxed immediately and transiently after heat shock (Mizushima, T., Natori, S. and Sekimizu, K., Mol. Gen. Genet. (1993) 238, 1–5). We next examined DNA relaxation and induction of heat shock proteins after heat shock in cells growing under anaerobic conditions. DNA in these cells relaxed rapidly (2 min) after heat shock (42°C), as was the case with aerobically growing cells, but full superhelicity was not recovered. The relaxed state of DNA topology was maintained for 60 min after heat shock. Induction of DnaK and GroEL proteins, which was transient in aerobically growing cells, was continuous in anaerobically growing cells. Therefore, induction of heat shock proteins correlated with DNA relaxation in both aerobic and anaerobic conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07122.x
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of DNA topoisomerases involved in immediate and transient DNA relaxation induced by heat shock inEscherichia coli (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 451-455 
    Details
    ISSN: 1617-4623
    Keywords: Heat shock ; DNA relaxation ; topA ; DNA topoisomerase I ; DNA gyrase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The linking number of plasmid DNA in exponentially growingEscherichia coli increases immediately and transiently after heat shock. The purpose of this study was to search for DNA topoisomerases that catalyze this relaxation of DNA. Neither introduction of atopA deletion mutation nor treatment of cells with DNA gyrase inhibitors affected the DNA relaxation induced by heat shock. Thus, DNA topoisomerase I and DNA gyrase are apparently not involved in the process. However, the reaction was inhibited by nalidixic acid or by oxolinic acid in thetopA mutant and the reaction was resistant to nalidixic acid in atopA mutant carrying, in addition, thenalA26 mutation. These results are interpreted as indicating that both DNA topoisomerase I and DNA gyrase are involved in the DNA relaxation induced by heat shock.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00583895
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  • 3
    Electronic Resource
    Electronic Resource
    Relaxation of supercoiled DNA associated with induction of heat shock proteins in Escherichia coli (1993)
    Springer
    Molecular genetics and genomics 238 (1993), S. 1-5 
    Details
    ISSN: 1617-4623
    Keywords: DNA relaxation ; DNA supercoiling ; DNA gyrase ; Heat shock response ; rpoH
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Heat treatment of wild-type Escherichia coli cells led to a transient relaxation of negatively supercoiled plasmid DNA and there was no recovery of DNA torsional strain in the DNA in gyrA mutant cells. After heat treatment, DnaK and GroEL proteins were synthesized continuously in the gyrA mutant cells, whereas they were synthesized only transiently in wild-type cells. Thus, change in superhelical density of the DNA correlated with the temperature-induced expression of heat shock proteins. Inhibitors of DNA gyrase (nalidixic acid, novobiocin), an organic solvent (ethanol) and a psychotropic drug (chlorpromazine) all stimulated relaxation of cellular DNA over the same concentration range that induces heat shock proteins. As DNA relaxation was induced by heat treatment or chemicals in an rpoH mutant, the process is not the result of induced synthesis of heat shock proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00279523
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    Paper (German National Licenses)
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