Plant Mitochondrial Cytochromes

Ducet, Gaston

doi:10.1007/978-3-642-70101-6_5

Cited by 3 publications

(1 citation statement)

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“…4) relieves the inhibition of total '^Pincorporation. Anaerobiosis causes the complete reduction of the electron transport chain and KCN treatment results in a chain where all components except cyto- chrome a, are reduced (Ducet 1985):; but the two treatments have little or no effect on phosphorylation during the standard assay time (Tab. 1, Fig.…”

Section: Discussionmentioning

confidence: 99%

Modulation of endogenous protein phosphorylation in plant mitochondria by respiratory substrates

Petit¹,

Sommarin²,

Pical³

1990

Physiol Plant

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Petit, P. X., Sommarin, M., Pical, C. and M0ller, I. M. 1990. Modulation of endogenous protein phosphorylation in plant mitochondria by respiratory substrates. Purified mitochondria from potato {Solanum tuberosum L. ev. Bintje) tubers were incubated with [y-'^F]-ATP, respiratory substrates and various effectors. The total incorporation of '^P into proteins was measured and the phosphoprotein pattern investigated by sodium dodecyl sulphate-polyacrylamide gel eleetrophoresis and autoradiography. Total incorporation was strongly reduced (by 70-80 %) by the respiratory substrates, succinate, pyruvate and NADH. The half-maximal inhibition was at 0.03, 0.3, and 0.3 mM, respectively. The labelling ofthe major phosphoproteins of 40 and 42 kDa (probably both the a-subtmit ofthe pyruvate dehydrogenase, EC 1.2.4.1) as well as of minor polypeptides of 26-33 kDa was reduced. A concomittant increase in the labelling of the 14 and 16 kDa bands occurred in the presence of succinate in fall but this increase could not be detected in late winter. The reduction' in total labelling caused by NADH and suecinate was unaffected by changes in the membrane potential (e.g. addition of uncouplers) or by inhibition of electron transport (e.g. by KCN). Malonate inhibition of succinate oxidation reversed the effects of succinate on labelling. The mechanism(s) by which respiratory substrates might affect protein kinase activity is discussed.

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Section: Discussionmentioning

confidence: 99%