Action of cytochalasin A, A sulfhydryl-reactive agent, on sugar metabolism and membrane-bound adenosine triphosphatase of yeast

  • Kuo S
  • Lampen J
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Abstract

Cytochalasin A at 10-20 μg/ml inhibits growth and sugar uptake by Saccharomyces strain 1016. The effects of cytochalasin A in intact cells were completely prevented when 1 mM cysteine or dithiothreitol was added along with cytochalasin A, but were not eliminated by thiols added after inhibition had occurred. Purified yeast hexokinase, glucose-6-P dehydrogenase, phosphofructokinase and aldolase were not sensitive to cytochalasin A (20 μg/ml). Glyceraldehyde-3-P dehydrogenase was strongly inhibited by cytochalasin A (5 μg/ml); activity was promptly restored by thiols. Anaerobic glycolysis was inhibited by cytochasasin A or by iodoacetate; unlike iodoacetate, cytochalasin A did not cause accumulation of sugar phosphates. In contrast, cytochalasin A, but not iodoacetate, inhibited isolated membrane-bound ATPases. Cytochalasin A is a sulfhydryl-reactive agent and has membrane-related effects (adenosine triphosphatase) which may well be the basis of its interference with energy-dependent uptake of solutes. © 1975.

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Authors

  • S. C. Kuo

  • J. Oliver Lampen

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