Effects of Methomyl and Helminthosporium maydis Toxin on Matrix Volume, Proton Motive Force, and NAD Accumulation in Maize (Zea mays L.) Mitochondria
Open Access
- 1 October 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 76 (2) , 508-517
- https://doi.org/10.1104/pp.76.2.508
Abstract
Methomyl and Helminthosporium maydis race T toxin block oxidative phosphorylation in mitochondria isolated from maize plants with Texas male sterile cytoplasm (T) but not in mitochondria isolated from those with Normal cytoplasm (N) (Bednarski, Izawa, Scheffer 1977 Plant Physiol 59: 540-545). Moreover, they have been reported to cause specific swelling in T mitochondria (Miller, Koeppe 1971 Science 173: 67-69; Koeppe, Cox, Malone 1978 Science 201: 1227-1229). We could not detect, by direct volume measurements, any change induced by these compounds in the mitochondrial matrix space. We show here that the proton motive force, which in maize mitochondria is composed of a large transmembrane potential and of a low transmembrane pH difference, is absent in T mitochondria incubated in the presence of methomyl or of Helminthosporium maydis race T toxin, while it is unchanged in N mitochondria. Methomyl and Helminthosporium maydis race T toxin induce, independently of the collapse of the proton motive force, a release of the cofactors NAD and coenzyme A from the mitochondrial matrix space. In particular, we show that NAD is transported in maize mitochondria, and that this transport, which is not dependent on the proton motive force, is inhibited by methomyl or Helminthosporium maydis race T toxin.Keywords
This publication has 14 references indexed in Scilit:
- Probes of membrane potential in Escherichia coli cellsFEBS Letters, 1981
- A comparison of the phosphorylation potential and electrochemical proton gradient in mung bean mitochondria and phosphorylating sub-mitochondrial particlesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1981
- Effect of NAD+ on Malate Oxidation in Intact Plant MitochondriaPlant Physiology, 1980
- A Comparison of Purified Host Specific Toxin from Helminthosporium maydis, Race T, and Its Acetate Derivative on Oxidation by Mitochondria from Susceptible and Resistant PlantsPlant Physiology, 1980
- Helminthosporium maydis Race T Toxin Induces Leakage of NAD+ from T Cytoplasm Corn MitochondriaPlant Physiology, 1979
- Mitochondrial Heredity: A Determinant in the Toxic Response of Maize to the Insecticide MethomylScience, 1978
- Inheritance of selected pathotoxin resistance in maize plants regenerated from cell culturesProceedings of the National Academy of Sciences, 1977
- Reversible Effects of Toxin from Helminthosporium maydis Race T on Oxidative Phosphorylation by Mitochondria from MaizePlant Physiology, 1977
- Southern Corn Leaf Blight: Susceptible and Resistant MitochondriaScience, 1971
- AN INVESTIGATION OF THE FREE AMINO GROUPS IN OXYTOCIN AND DESULFURIZED OXYTOCIN PREPARATIONSJournal of Biological Chemistry, 1951