Isolation and properties of an ATP transporter from a strain of Aspergillus niger

A purified ATP transporter from Aspergillus niger did not show release or uptake for any of the nucleotides (ADP or UTP) except ATP. The release and uptake did not result from non-specific binding, but appeared to be concentration-dependent processes. ATP was shown by a double-isotopic technique to be transported across membrane vesicles without degradation. The ATP-transport protein was purified to near homogeneity from the membrane vesicles of a strain of A. niger and its apparent M-r was approximately 60 000. The purified protein showed the properties of a membrane-bound protein in that the carrier protein was shown, during the liposome-preparative process, to translocate from the aqueous phase into the lipid bilayer of the liposome, unlike the cytosolic protein glucose-6-phosphate dehydrogenase, which remained confined to the aqueous compartment. Mycobacillin, a lipid-reactive antibiotic, was bound to the transport protein at a site other than the ATP-binding site, leading to its enhanced release or uptake, which was very feeble in absence of the antibiotic.