Coupling factor ATPase from Escherichia coli. An uncA mutant (uncA401) with defective .ALPHA. subunit.:An <i>UncA</i> Mutant (<i>uncA401</i>) with Defective α Subunit

J-STAGE
  • KANAZAWA Hiroshi
    Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University
  • SAITO Setsuo
    Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University
  • FUTAI Masamitsu
    Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University

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説明

Inactive coupling factor ATPase (F1) was prepared from an uncoupled mutant (uncA401) of Escherichia coli. Reconstitution of ATPase activity was observed when α subunit from wild-type F1 was added to the dissociated inactive F1 and the mixture was dialyzed against buffer containing ATP and Mg2+. ATPase was also reconstituted when the mixture of α subunit (wild type) and crude extract from the mutant was dialyzed against the same buffer. These results indicate that the mutant is defective in α subunit, suggesting that the uncA401 locus carries the structural gene for α subunit, and that this polypeptide plays an essential role in ATPase activity in F1, molecule.

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