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J Biol Chem, Vol. 273, Issue 35, 22173-22176, August 28, 1998

COMMUNICATION
Biochemical Characterization of the Human Arsenite-stimulated ATPase (hASNA-I)

Buran Kurdi-Haidar, Dennis Heath, Stephan Aebi^¶, and Stephen B. Howell

From the  Department of Medicine and the University of California, San Diego Cancer Center, University of California, San Diego, La Jolla, California 92093-0058 and the ^¶ Department of Medical Oncology, University of Bern, Inselspital CH-3010 Bern, Switzerland

Arsenic is a potent toxin and carcinogen. In prokaryotes, arsenic detoxification is accomplished by chromosomal and plasmid-borne operon-encoded efflux systems. We have previously reported the cloning of hASNA-I, a human homologue of arsA encoding the ATPase component of the Escherichia coli arsenite transporter. Purified glutathione S-transferase (GST)-hASNA-I fusion protein was biochemically characterized, and its properties were compared with those of ArsA. The GST-hASNA-I exhibited a basal level of ATPase activity of 18.5 ± 8 nmol/min/mg in the absence of arsenite. Arsenite produced a 1.6 ± 0.1-fold stimulation of activity (p = 0.0044), which was related to an increase in V_max; antimonite did not stimulate activity. Two lines of evidence suggest that an oligomer is the most likely native form of hASNA-I. First, lysates of human embryo kidney 293 cells overproducing recombinant hASNA-I produced a single monomeric 37-kDa band on SDS-polyacrylamide gel electrophoresis (PAGE) and two distinct species when analyzed using nondenaturing PAGE. Second, chemical cross-linking of the 63-kDa GST-hASNA-I resulted in the formation of dimeric and tetrameric protein forms. The results indicate that hASNA-I is a distinct human arsenite-stimulated ATPase belonging to the same superfamily of ATPases represented by the E. coli ArsA protein.

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