Abstract:
:Intracellular copper routing in Enterococcus hirae is accomplished by the CopZ copper chaperone. Under copper stress, CopZ donates Cu(+) to the CopY repressor, thereby releasing its bound zinc and abolishing repressor-DNA interaction. This in turn induces the expression of the cop operon, which encodes CopY and CopZ, in addition to two copper ATPases, CopA and CopB. To gain further insight into the function of CopZ, the yeast two-hybrid system was used to screen for proteins interacting with the copper chaperone. This led to the identification of Gls24, a member of a family of stress response proteins. Gls24 is part of an operon containing eight genes. The operon was induced by a range of stress conditions, but most notably by copper. Gls24 was overexpressed and purified, and was shown by surface plasmon resonance analysis to also interact with CopZ in vitro. Circular dichroism measurements revealed that Gls24 is partially unstructured. The current findings establish a novel link between Gls24 and copper homeostasis.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Stoyanov JV,Mancini S,Lu ZH,Mourlane F,Poulsen KR,Wimmer R,Solioz Mdoi
10.1111/j.1574-6968.2009.01833.xsubject
Has Abstractpub_date
2010-01-01 00:00:00pages
69-75issue
1eissn
0378-1097issn
1574-6968pii
FML1833journal_volume
302pub_type
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