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Endogenous elemental sulfur production froml-cysteine in dormant α-spores ofPhomopsis viticola

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Abstract

The enzymatic production of sulfur froml-cysteine was studied in young dormant α-spores ofPhomopsis viticola. Cysteine aminotransferase (CAT) and mercaptopyruvate sulfurtransferase (MST) activities could be responsible for the production of endogenous elemental sulfur (S0) in α-spores.l-Cysteine was first deaminated, with production of β-mercaptopyruvate, by the CAT. The β-mercaptopyruvate produced is successively desulfurated by the MST with production of sulfur and pyruvate. Deaminase activity was recovered principally in the cytoplasmic fraction, whereas desulfurase activity was recovered mainly in the mitochondrial fraction.l-Cysteine and S0 sharply affected the respiratory activity, the ATP content, and suppressed germination of α-spores. In contrast, reduced glutathione did not affect these metabolic parameters. Production of S0 by enzymatic degradation ofl-cysteine could be responsible for the inhibitory action of this amino acid. We suggest that CAT and MST, by their capacity to produce sulfur or S0, plays a key role in regulation of morphogenetic processes ofPhomopsis viticola.

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Authors and Affiliations

  1. Laboratory of General Microbiology, Department of Plant Biology, University of Geneva, Switzerland

    Trello Beffa & Gilbert Turian

  2. Federal Station of Agronomic Research in Changins, Nyon, Switzerland

    Roger Pezet

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  1. Trello Beffa
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  2. Roger Pezet
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  3. Gilbert Turian
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Beffa, T., Pezet, R. & Turian, G. Endogenous elemental sulfur production froml-cysteine in dormant α-spores ofPhomopsis viticola . Current Microbiology 17, 259–263 (1988). https://doi.org/10.1007/BF01571325

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