Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase (original) (raw)

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Mitochondrial copper metabolism is crucial for cellular respiration, particularly in the assembly of cytochrome c oxidase, a key enzyme in the electron transport chain. This study identifies essential amino acids in the yeast protein Sco1p, demonstrating that specific cysteine residues are critical for its function in copper transfer, thereby enhancing our understanding of mitochondrial copper metabolism and its implications for respiratory function.

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Abstract

Saccharomyces cerevisiae Sco1p is believed to be involved in the transfer of copper from the carrier Cox17p to the mitochondrial cytochrome c oxidase subunits 1 and 2. We here report on the results of a mutational analysis of Sco1p. The two cysteine residues of a potential metal-binding motif (CxxxC) are essential for protein function as shown by their substitution by alanines. Chimeras consisting of Sco1p and its homolog S. cerevisiae Sco2p restrict the specificity of Sco1p function to the N-terminal half of the protein. A candidate region for conferring specificity on Sco1p is a stretch of hydrophobic amino acids, which act as a membrane anchor. In line with this suggestion is the result that alterations of individual amino acids within this region impair Sco1p function.

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Authors and Affiliations

  1. Institut für Genetik, Technische Universität Dresden, Mommsenstraße 13, D-01062 Dresden, Germany e-mail: Gerhard.Roedel@mailbox.tu-dresden.de Tel.: +49-351-4633010 Fax: +49-351-4637725, , , , , , DE
    Anja Rentzsch, Gaby Krummeck-Weiß, Angelika Hofer, Anne Bartuschka, K. Ostermann & G. Rödel

Authors

  1. Anja Rentzsch
  2. Gaby Krummeck-Weiß
  3. Angelika Hofer
  4. Anne Bartuschka
  5. K. Ostermann
  6. G. Rödel

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Received: 30 October / 10 December 1998

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Rentzsch, A., Krummeck-Weiß, G., Hofer, A. et al. Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase.Curr Genet 35, 103–108 (1999). https://doi.org/10.1007/s002940050438

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