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J Biol Chem, Vol. 273, Issue 34, 21455-21462, August 21, 1998

Prodigiosins as a New Group of H⁺/Cl Symporters That Uncouple Proton Translocators

Tomohiko Sato, Hiroki Konno, Yasufumi Tanaka, Takao Kataoka^§, Kazuo Nagai^§, Harry H. Wasserman^¶, and Shoji Ohkuma

From the  Laboratory of Biochemistry, Department of Molecular and Cell Biology, Faculty of Pharmaceutical Sciences, Kanazawa University, Takara-machi 13-1, Kanazawa, Ishikawa 920-0934, Japan, the ^§ Department of Bioengineering, Tokyo Institute of Technology, Nagatsuta-chou 4259, Midori-ku, Yokohama, Kanagawa 226-0026, Japan, and the ^¶ Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107

We reported previously (Kataoka, T., Muroi, M., Ohkuma, S., Waritani, T., Magae, J., Takatsuki, A., Kondo, S., Yamasaki, M., and Nagai, K. (1995) FEBS Lett. 359, 53-59) that prodigiosin 25-C uncoupled vacuolar H⁺-ATPase, inhibited vacuolar acidification, and affected glycoprotein processing. In the present study we show that prodigiosins (prodigiosin, metacycloprodigiosin, and prodigiosin 25-C) inhibit the acidification activity of H⁺-ATPase chloride dependently, but not membrane potential formation or ATP hydrolysis activity, and suggest that they promote H⁺/Cl symport (or OH/Cl exchange, in its equivalence) across vesicular membranes. In fact, prodigiosins displayed H⁺/Cl symport activity on liposomal membranes. First of all, they decreased the internal pH of liposomes depending on the external chloride, and raised it depending on the internal chloride when external buffer was free from chloride. Second, their effect was electroneutral and not seriously affected by the application of an inside positive membrane potential generated by K⁺ and valinomycin. Finally, they promoted the uptake of [³⁶Cl] from external buffers with concomitant intraliposomal acidification when external pH was acidic relative to liposome interior. As prodigiosins hardly inhibit the catalytic activity (ATP hydrolysis) unlike well known OH/Cl exchangers (for example, tributyltin chloride), they should provide powerful tools for the study of molecular machinery and cellular activities involving transport of protons and/or chloride.

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