YCF1-mediated cadmium resistance in yeast is dependent on copper metabolism and antioxidant enzymes.

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  • Author(s): Wei W;Wei W; Smith N; Wu X; Kim H; Seravalli J; Khalimonchuk O; Lee J
  • Source:
    Antioxidants & redox signaling [Antioxid Redox Signal] 2014 Oct 01; Vol. 21 (10), pp. 1475-89. Date of Electronic Publication: 2014 Feb 25.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Mary Ann Liebert, Inc Country of Publication: United States NLM ID: 100888899 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1557-7716 (Electronic) Linking ISSN: 15230864 NLM ISO Abbreviation: Antioxid Redox Signal Subsets: MEDLINE
    • Publication Information:
      Original Publication: Larchmont, NY : Mary Ann Liebert, Inc., 1999-
    • Subject Terms:
      ATP-Binding Cassette Transporters/*physiology ; Antioxidants/*metabolism ; Cadmium/*toxicity ; Copper/*metabolism ; Saccharomyces cerevisiae Proteins/*physiology ; Superoxide Dismutase/*metabolism; Drug Resistance, Fungal ; Oxidative Stress
    • Abstract:
      Aims: Acquisition and detoxification of metal ions are vital biological processes. Given the requirement of metallochaperones in cellular copper distribution and metallation of cuproproteins, this study investigates whether the metallochaperones also deliver metal ions for transporters functioning in metal detoxification.
      Results: Resistance to excess cadmium and copper of the yeast Saccharomyces cerevisiae, which is conferred by PCA1 and CaCRP1 metal efflux P-type ATPases, respectively, does not rely on known metallochaperones, Atx1p, Ccs1p, and Cox17p. Copper deficiency induced by the expression of CaCRP1 encoding a copper exporter occurs in the absence of Atx1p. Intriguingly, CCS1 encoding the copper chaperone for superoxide dismutase 1 (Sod1p) is necessary for cadmium resistance that is mediated by Ycf1p, a vacuolar cadmium sequestration transporter. This is attributed to Ccs1p's role in the maturation of Sod1p rather than its direct interaction with Ycf1p for cadmium transfer. Functional defect in Ycf1p associated with the absence of Sod1p as well as another antioxidant enzyme Glr1p is rescued by anaerobic growth or substitutions of specific cysteine residues of Ycf1p to alanine or serine. This further supports oxidative inactivation of Ycf1p in the absence of Ccs1p, Sod1p, or Glr1p.
      Innovation: These results provide new insights into the mechanisms of metal metabolism, interaction among metal ions, and the roles for antioxidant systems in metal detoxification.
      Conclusion: Copper metabolism and antioxidant enzymes maintain the function of Ycf1p for cadmium defense.
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    • Grant Information:
      P30 GM103335 United States GM NIGMS NIH HHS; DK79209 United States DK NIDDK NIH HHS; P30RM103335 United States RM RMOD NIH HHS; ES16337 United States ES NIEHS NIH HHS
    • Accession Number:
      0 (ATP-Binding Cassette Transporters)
      0 (Antioxidants)
      0 (Saccharomyces cerevisiae Proteins)
      0 (YCF1 protein, S cerevisiae)
      00BH33GNGH (Cadmium)
      789U1901C5 (Copper)
      EC 1.15.1.1 (Superoxide Dismutase)
    • Publication Date:
      Date Created: 20140122 Date Completed: 20150515 Latest Revision: 20211021
    • Publication Date:
      20240829
    • Accession Number:
      PMC4158973
    • Accession Number:
      10.1089/ars.2013.5436
    • Accession Number:
      24444374