作者: Naoki Nakada , Hans Gmünder , Takahiro Hirata , Mikio Arisawa
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摘要: The mechanism of inhibition DNA gyrase by cyclothialidine, a novel inhibitor isolated from Streptomyces filipinensis NR0484, has been studied further using [14C]benzoylcyclothialidine and reconstituted Escherichia coli system consisting the A subunit, B subunit relaxed ColE1 DNA. was also with 43-kDa N-terminal fragment subunit. could bind to alone but not nor plasmid alone. Furthermore, compound bound Scatchard analysis binding showed that affinity increased, depending on assembly (A2B2)·DNA complex. This suggests site cyclothialidine or its vicinity causes conformational change during gyrase·DNA complex (increase in affinity: → A2B2 A2B2·DNA). displacement curves nonlabeled ATP analogues, coumarin antibiotics indicated coumarins, share common (or overlapping) action gyrase; however, microenvironment sites may differ.