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

Stoyanov, Jivko V; Mancini, Stefano; Lu, Zen Huat; Mourlane, Frédéric; Poulsen, Kristian R; Wimmer, Reinhard; Solioz, Marc (2010). The stress response protein Gls24 is induced by copper and interacts with the CopZ copper chaperone of Enterococcus hirae. FEMS microbiology letters, 302(1), pp. 69-75. Malden, Mass.: Blackwell Publishing Ltd 10.1111/j.1574-6968.2009.01833.x

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Gastro-intestinal, Liver and Lung Disorders (DMLL) > Clinic of Visceral Surgery and Medicine > Hepatology

UniBE Contributor:

Solioz, Marc

ISSN:

0378-1097

Publisher:

Blackwell Publishing Ltd

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:11

Last Modified:

21 Nov 2019 03:32

Publisher DOI:

10.1111/j.1574-6968.2009.01833.x

PubMed ID:

19903200

Web of Science ID:

000272171900010

BORIS DOI:

10.7892/boris.1742

URI:

https://boris.unibe.ch/id/eprint/1742 (FactScience: 203682)

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