The copper chaperone for superoxide dismutase

Valeria Cizewski Culotta, Leo W.J. Klomp, Jeffrey Strain, Ruby Leah B. Casareno, Bernhard Krems, Jonathan D. Gitlin

Research output: Contribution to journalArticle

Abstract

Copper is distributed to distinct localizations in the cell through diverse pathways. We demonstrate here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated through a soluble factor identified as Saccharomyces cerevisiae LYS7 and human CCS (copper chaperone for SOD). This factor is specific for SOD1 and does not deliver copper to proteins in the mitochondria, nucleus, or secretory pathway. Yeast cells containing a lys7Δ null mutation have normal levels of SOD1 protein, but fail to incorporate copper into SOD1, which is therefore devoid of superoxide scavenging activity. LYS7 and CCS specifically restore the biosynthesis of holoSOD1 in vivo. Elucidation of the CCS copper delivery pathway may permit development of novel therapeutic approaches to human diseases that involve SOD1, including amyotrophic lateral sclerosis.

Original languageEnglish (US)
Pages (from-to)23469-23472
Number of pages4
JournalJournal of Biological Chemistry
Volume272
Issue number38
DOIs
StatePublished - Sep 19 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Culotta, V. C., Klomp, L. W. J., Strain, J., Casareno, R. L. B., Krems, B., & Gitlin, J. D. (1997). The copper chaperone for superoxide dismutase. Journal of Biological Chemistry, 272(38), 23469-23472. https://doi.org/10.1074/jbc.272.38.23469