Metallation state of human manganese superoxide dismutase expressed in Saccharomyces cerevisiae.

ABSTRACT: Human manganese superoxide dismutase (Sod2p) has been expressed in yeast and the protein purified from isolated yeast mitochondria, yielding both the metallated protein and the less stable apoprotein in a single chromatographic step. At 30 °C growth temperature, more than half of the purified enzyme is apoprotein that can be fully activated following reconstitution, while the remainder contains a mixture of manganese and iron. In contrast, only fully metallated enzyme was isolated from a similarly constructed yeast strain expressing the homologous yeast manganese superoxide dismutase. Both the manganese content and superoxide dismutase activity of the recombinant human enzyme increased with increasing growth temperatures. The dependence of in vivo metallation state on growth temperature re

SUBMITTER: Whittaker MM 

PROVIDER: S-EPMC3369014 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature