The influence of salicylic acid (SA) on generation of membrane potential (Δψ) at the inner membrane of isolated mitochondria from cotyledons of lupine seedlings (Lupinus angustifolius L.) was investigated. The mitochondrial preparations conformed to all criteria of the intactness: the organelles were characterized by the integrity of their membranes and by tight coupling of oxidation and phosphorylation. High functional activity of mitochondria was also evident from their ability to generate Δψ during succinate oxidation and from the long-term maintenance of steady-state transmembrane potential by virtue of electrontransport chain (ETC) operation or ATP hydrolysis after the inhibition of respiratory ETC. The addition of SA to the incubation medium (0.5–1.0 mM) induced a fast and complete dissipation of Δψ after a distinct lag period. The Δψ was not restored by subsequent ATP hydrolysis, indicating that the phytohormone SA induced the proton conductance of the inner membrane. The SA-induced collapse of Δψ was observed under suppression of ETC by anaerobiosis, cyanide, or inhibitory concentrations of the phytohormone. The SAinduced dissipation of Δψ was not reversed by cyclosporine A but was prevented in the presence of dithiothreitol (DTT). Conversely, the incubation of mitochondria in the presence of phenylarsine oxide (PAO) known to oxidize the protein thiol groups also elevated the proton conductance and eliminated Δψ at the inner membrane of lupine mitochondria. The PAO-induced Δψ collapse was not reversed in the presence of ATP, but Δψ was restored after the addition of DTT. These results and the literature data suggest that, under suppressed ETC activity, salicylic acid permeabilizes the inner membrane of mitochondria from cotyledons of lupine seedlings due to opening of a specialized mitochondrial uncoupling channel (MUC) that is permeable to protons and, possibly, to other small cations (K+, Ca2+). An important role in the induction of MUC belongs apparently to oxidative stress resulting in oxidation of thiol groups in protein molecules that constitute this channel or regulate the channel activity.
Russian Journal of Plant Physiology – Springer Journals
Published: Oct 19, 2016
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