The stress response protein Gls24 is induced by copper and interacts with the CopZ copper chaperone of Enterococcus hirae.

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 Lett

authors

Stoyanov JV,Mancini S,Lu ZH,Mourlane F,Poulsen KR,Wimmer R,Solioz M

doi

10.1111/j.1574-6968.2009.01833.x

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

69-75

issue

1

eissn

0378-1097

issn

1574-6968

pii

FML1833

journal_volume

302

pub_type

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