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Catabolite inactivation, cyclic AMP and protein phosphorylation in the methylotrophic yeastHansenula polymorpha

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Abstract

The inactivation of the peroxisomal enzyme alcohol oxidase and the cytoplasmic enzymes fructose-1,6-bisphosphatase, malate dehydrogenase and phosphoenolpyruvate carboxykinase was found to occur after addition of glucose to methanol-grown cells of the yeastHansenula polymorpha. The concentration of cyclic AMP increased nearly twofold within 3 min under the same conditions. In crude extracts ofH. polymorpha about 20 proteins are phosphorylated by cyclic AMP dependent protein kinases, among them also fructose-1,6-bisphosphatase. No phosphorylation of the alcohol oxidase protein could be detected. From this fact, it was concluded that the inactivation of the peroxisomal alcohol oxidase is independent of cyclic AMP-dependent protein phosphorylation.

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  1. Institut für Angewandte und Technische Mikrobiologie, Ernst-Moritz-Arndt-Universität Greifswald, 0-2200, Greifswald, Germany

    Klaus H. Hofmann & Elke Polnisch

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  1. Klaus H. Hofmann
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  2. Elke Polnisch
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Hofmann, K.H., Polnisch, E. Catabolite inactivation, cyclic AMP and protein phosphorylation in the methylotrophic yeastHansenula polymorpha . Antonie van Leeuwenhoek 60, 49–54 (1991). https://doi.org/10.1007/BF00580441

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  • DOI: https://doi.org/10.1007/BF00580441

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