Cercospora beticola toxins. Part XVII. The role of beticolin/Mg2+ complexes in their biological activity. Study of plasma membrane H+-ATPase, vacuolar H+-PPase, alkaline and acid phosphatases

Beticolin-1 and beticolin-2, yellow toxins produced by the phytopathogenic fungus Cercospora beticola, inhibit the plasma membrane H+-ATPase. Firstly, since beticolins are able to form complexes with Mg2+, the role of the beticolin/Mg2+ complexes in the inhibition of the plasma membrane proton pump has been investigated. Calculations indicate that beticolins could exist under several forms, in the H+-ATPase assay mixture, both free or complexed with Mg2+. However, the percentage inhibition of the H+-ATPase activity is correlated to the concentration of one single form of beticolin, the dimeric neutral complex Mg2H2B2, which appears to be the active form involved in the H+-ATPase inhibition. Secondly, since previous data suggested that beticolins could also be active against other Mg2+-dependent enzymes, we tested beticolin-1 on the vacoular H+-PPase, which requires Mg2+ as co-substrate, and on the alkaline and acid phosphatases, which do not use Mg2+ as co-substrate. Only vacuolar H+-PPase is sensitive to beticolin-1, which suggests that beticolins are specific to enzymes that use a complex of Mg2+ as the substrate. The same Mg2H2B2 complex which is responsible of the plasma membrane H+-ATPase inhibition appears to be also involved in the inhibition of the vacuolar H+-PPase.