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Nucleic Acids Research, 1981, Vol. 9, No. 8 1949-1961
© 1981

ENZYMOLOGY

Properties of a DNA-dependent ATPase from rat mitochondria

Katsuyuki Yaginuma and Katsuro Koike

Cancer Institute, Japanese Foundation for Cancer Research Kami-Ikebukuro, Toshima-ku, Tokyo 170, Japan

Received February 24, 1981. A DNA-dependent ATPase has been highly purified from rat liver mitochondria and characterized. The enzyme catalyzes the hydrolysis of ATP or dATP in the presence of single-stranded DNA cofactor and a divalent cation. The Km values for ATP and dATP are 0.15 mM and 0.35 mM, respectively. The enzyme activity is highly sensitive to N-ethylmaleimide. The sedimentation coefficient of the enzyme is 8.3 S in a glycerol gradient. From this and data on Sephadex G-200 gel filtration, the molecular weight of the native enzyme was calculated to be about 190,000. All the natural single-stranded DNAs tested were equally effective for the ATPase activity, but synthetic deoxyhomopolymer poly(dC) was found to be more effective than natural single-stranded DNAs. Synthetic and natural RNAs had no effect on the activity.


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