Sensitivity of the aldehyde-induced and free fatty acid-induced activities of plant uncoupling protein to GTP is regulated by the ubiquinone reduction level.
الكلمات الدالة
نبذة مختصرة
Using isolated potato tuber mitochondria possessing uncoupling protein (StUCP), we found that, under non-phosphorylating conditions, the sensitivity of aldehyde (all trans-retinal or 4-hydroxy-2-nonenal)-induced and fatty acid (linoleic acid)-induced StUCP-mediated proton leaks to GTP is controlled by the endogenous ubiquinone (Q) reduction level. The action of StUCP activators was abolished by GTP only when Q was sufficiently oxidized, but no inhibitory effect was observed when Q was highly reduced. Thus, the Q reduction level-dependent regulation of StUCP inhibition functions independently of the type of UCP activation and could be an important physiological factor affecting the efficiency of UCP-catalyzed uncoupling in plant mitochondria.