Yeast copper-zinc superoxide dismutase can be activated in the absence of its copper chaperone
| Autor: | Sea, Kevin W, Sheng, Yuewei, Lelie, Herman L, Kane Barnese, Lindsay, Durazo, Armando, Valentine, Joan Selverstone, Gralla, Edith Butler |
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| Rok vydání: | 2013 |
| Předmět: |
Disulfide bond
Superoxide Dismutase Biophysics Copper chaperone Saccharomyces cerevisiae Neurodegenerative Sod1 Copper transport Enzyme Activation Inorganic Chemistry Zinc Medicinal and Biomolecular Chemistry Superoxide Dismutase-1 Rare Diseases CCS1 Biochemistry and Cell Biology Oxidation-Reduction Copper |
| Zdroj: | Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, vol 18, iss 8 |
| Popis: | Copper-zinc superoxide dismutase (Sod1) is an abundant intracellular enzyme that catalyzes the disproportionation of superoxide to give hydrogen peroxide and dioxygen. In most organisms, Sod1 acquires copper by a combination of two pathways, one dependent on the copper chaperone for Sod1 (CCS), and the other independent of CCS. Examples have been reported of two exceptions: Saccharomyces cerevisiae, in which Sod1 appeared to be fully dependent on CCS, and Caenorhabditis elegans, in which Sod1 was completely independent of CCS. Here, however, using overexpressed Sod1, we show there is also a significant amount of CCS-independent activation of S. cerevisiae Sod1, even in low-copper medium. In addition, we show CCS-independent oxidation of the disulfide bond in S. cerevisiae Sod1. There appears to be a continuum between CCS-dependent and CCS-independent activation of Sod1, with yeast falling near but not at the CCS-dependent end. |
| Databáze: | OpenAIRE |
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