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Copper is required for prion protein‐associated superoxide dismutase‐l activity in Pichia pastoris
Author(s) -
Treiber Carina,
Pipkorn Rüdiger,
Weise Christoph,
Holland Gudrun,
Multhaup Gerd
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.05678.x
Subject(s) - pichia pastoris , superoxide dismutase , metalloprotein , biochemistry , reactive oxygen species , chemistry , dismutase , copper , intracellular , superoxide , yeast , copper protein , protease , enzyme , gene , recombinant dna , organic chemistry
The prion protein (PrP) is the key protein implicated in transmissible spongiform encephalopathies. It is a metalloprotein that binds manganese and copper. The latter is involved in the physiological function of the protein. We have previously found that PrP expression in Pichia pastoris affects intracellular metal ion concentrations and that formation of protease‐resistant PrP is induced by additional copper and/or manganese. In this study, we show that heterologously expressed PrP is post‐translationally modified and transported to the cell wall. We found by combining three different test systems that PrP itself had gained superoxide dismutase‐like activity in P. pastoris. However, this activity could not be inhibited by KCN and depended on additional copper in the medium. Thus, this study defines the conditions under which PrP exhibits superoxide dismutase‐like activity by showing that copper must be present for the protein to participate in scavenging and detoxification of reactive oxygen species.