Open AccessCopper homeostasis in Enterococcus hirae
Author(s) -
Solioz Marc,
Stoyanov Jivko V
Publication year - 2003
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1016/s0168-6445(03)00053-6
Subject(s) - enterococcus hirae , operon , biology , chaperone (clinical) , repressor , copper , atpase , two component regulatory system , genetics , gene , microbiology and biotechnology , bacteria , biochemistry , enterococcus , escherichia coli , gene expression , mutant , enzyme , chemistry , medicine , organic chemistry , pathology
Copper is an essential component of life because of its convenient redox potential of 200–800 mV when bound to protein. Extensive insight into copper homeostasis has only emerged in the last decade and Enterococcus hirae has served as a paradigm for many aspects of the process. The cop operon of E. hirae regulates copper uptake, availability, and export. It consists of four genes that encode a repressor, CopY, a copper chaperone, CopZ, and two CPx‐type copper ATPases, CopA and CopB. Most of these components have been conserved across the three evolutionary kingdoms. The four Cop proteins have been studied in vivo as well as in vitro and their function is understood in some detail.