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J. Biol. Chem., Vol. 277, Issue 8, 5944-5951, February 22, 2002
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From the Department of Biochemistry, Duke University Medical
Center, Durham, North Carolina 27710
We have prepared full-length
Drosophila and human topoisomerase II and truncation
constructs containing the amino-terminal ATPase domain, and we have
analyzed their biochemical properties. The ATPase activity of the
truncation proteins, similar to that of the full-length proteins, is
greatly stimulated by the presence of DNA. This activity of the
truncation proteins is also sensitive to the inhibition by the drug
bisdioxopiperazine, ICRF-193, albeit at a much lower level than the
full-length protein. Therefore, bisdioxopiperazine can directly
interact with the NH2-terminal ATPase domain, but the
drug-enzyme interaction may involve other domains as well. The ATPase
activity of the ATPase domain protein showed a quadratic dependence on
enzyme concentration, suggesting that dimerization of the
NH2-terminal domain is a rate-limiting step. Using both
protein cross-linking and sedimentation equilibrium analysis, we showed
that the ATPase domain exists as a monomer in the absence of cofactors
but can readily dimerize in the presence of a nonhydrolyzable analog of
ATP, 5'-adenylyl-
,
-imidodiphosphate. More interestingly,
both ATP and ADP can also promote protein dimerization. This result
thus suggests that the protein clamp, mediated through the dimerization
of ATPase domain, remains closed after ATP hydrolysis and opens upon
the dissociation of ADP.
To whom correspondence should be addressed. Fax: 919-684-8885;
E-mail: Hsieh@biochem.duke.edu.
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