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J. Biol. Chem., Vol. 266, Issue 6, 3540-3546, Feb, 1991
RJ Reece and A Maxwell
In a previous report (Reece, R. J., and Maxwell, A. (1989) J. Biol. Chem.
264, 19648-19653) we showed that treatment of the Escherichia coli DNA
gyrase A protein with trypsin generates two stable fragments. The
N-terminal 64-kDa fragment supports DNA supercoiling, while the C- terminal
33-kDa fragment shows no enzymic activity. We proposed that the 64-kDa
fragment represents the DNA breakage-reunion domain of the A protein. We
have now engineered the gyrA gene such that the 64-kDa protein is generated
as a gene product. The properties of this protein confirm the findings of
the experiments with the 64-kDa tryptic fragment. We have also generated a
series of deletions of the gyrA gene such that C-terminal and N-terminal
truncated versions of the A protein are produced. The smallest of the
N-terminal fragments found to be able to carry out the DNA breakage-reunion
reaction is GyrA(1-523). The cleavage reaction mediated by this protein
occurs with equal efficacy as that performed by the intact GyrA protein.
Deletion of the N- terminal 6 amino acids from either the A protein or
these deletion derivatives has no effect on enzymic activity, while
deletion of the N- terminal 69 amino acids completely abolishes the DNA
breakage-reunion reaction. Therefore the smallest GyrA protein we have
found that will perform DNA breakage and reunion is GyrA(7-523). A model is
proposed for the domain organization of the gyrase A protein.
Probing the limits of the DNA breakage-reunion domain of the Escherichia coli DNA gyrase A protein
Department of Biochemistry, University of Leicester, United Kingdom.
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