The cop operon of Enterococcus hirae controls cytoplasmic copper levels. It encodes two copper ATPases, a repressor, and the CopZ metallo-chaperone. Transcription of these genes is induced by copper. However, at higher copper concentrations, CopZ is degraded by a copper-activated proteolytic activity. This specific proteolysis of CopZ can also be demonstrated in vitro with E. hirae extracts. Growth of the cells in copper increases the copper-inducible proteolytic activity in extracts. Zymography reveals the presence of a copper-dependent protease in crude cell lysates. Copper-stimulated proteolysis of CopZ appears to play an important role in copper homoeostasis by E. hirae.
Conference Article| August 01 2002
Role of proteolysis in copper homoeostasis
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M. Solioz; Role of proteolysis in copper homoeostasis. Biochem Soc Trans 1 August 2002; 30 (4): 688–691. doi: https://doi.org/10.1042/bst0300688
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