ATPase state and activity in thylakoids from normal and waterstressed lupin

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Abstract
To compare with the case of phosphorylation, ATP hydrolysis was investigated in thylakoids from plants submitted to drought. For medium stresses the relationship between hydrolysis rate and deactivation constant of the de-energized enzyme when Δph varies is unchanged, hence the basic mechanisms are preserved; (PSI-driven) energization then is neither affected, at any light intensity. As drought intensifies, hydrolysis and monogalactolipids fall somewhat in parallel. whereas the deactivation constant changes with digalactolipids and phosphatidic acid content. This alteration of the F0 lipid environment must be transduced to F1, the subunits of which, however, are preserved, as shown by LDS-PAGE, ATP synthesis (thiol-oxidized enzyme) and hydrolysis (thiol-reduced enzyme) show an identical decrease with stress. Thus the latter impairs a common early step, probably the activation of the oxidized enzyme