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Plant Physiology 65:785-791 (1980)
© 1980 American Society of Plant Biologists

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A Comparison of Purified Host Specific Toxin from Helminthosporium maydis, Race T, and Its Acetate Derivative on Oxidation by Mitochondria from Susceptible and Resistant Plants 1

Gary Payne2, Y. Kono3 and J. M. Daly

Laboratory of Agricultural Biochemistry, University of Nebraska, Lincoln, Nebraska 68583

NADH or succinate oxidation and malate oxidation were differentially affected in mitochondria from both susceptible and resistant corn by a purified and chemically characterized preparation of host-specific toxin from Bipolaris (Helminthosporium) maydis, race T. NADH and succinate oxidation by susceptible T corn mitochondria were stimulated 50 to 200% with apparent uncoupling from the cytochrome chain at ~=10–9M toxin (5 to 20 ng/ml). Significant inhibition of malate oxidation was observed at slightly higher toxin concentrations, but oxidation was still coupled to ADP utilization. Inhibition of malate oxidation also was observed in N corn (resistant) and soybean mitochondria at ~=1,000-fold greater concentrations, but stimulation of NADH and succinate oxidation was not found at any toxin concentration tested.

A fully acetylated toxin derivative at ~=1 microgram per milliliter also caused stimulation of NADH or succinate oxidation in T corn mitochondria, but not those of N corn or soybean mitochondria at 100 micrograms per milliliter. Malate oxidation was inhibited to the same extent by toxin acetate with mitochondria from T corn, N corn, and soybean. The blocking of hydroxyl groups in race T toxin by acetyl functions eliminated selectivity toward malate oxidation only. The data suggest that inhibition of malate oxidation is either a separate or secondary effect of selective action of toxin on T corn mitochondria, perhaps by interference with transport in or out of the matrix. Sensitivity of T, but not N, corn mitochondria to purified toxin decays within minutes after pellets are suspended in aqueous osmotica, with no obvious change in mitochondrial integrity. The action of race T toxin seems to involve a labile process, such as ion gradient(s), or an unstable structural conformation of T corn mitochondria.


2 Present address: Department of Plant Pathology, North Carolina State University, Raleigh, North Carolina 27650.

3 Present address: Institute of Physical and Chemical Research, Wako-Shi, Saitama 351 Japan.

1 Published as Paper No. 5847, Journal Series, Nebraska Agricultural Experiment Station. Supported in part by Cooperative States Research Service Special Grant 216-15-22.




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