Interaction between cyanobacterial copper chaperone Atx1 and zinc homeostasis

JBIC Journal of Biological Inorganic Chemistry - Tập 15 - Trang 77-85 - 2009
Samantha J. Dainty1, Carl J. Patterson1, Kevin J. Waldron1, Nigel J. Robinson1
1Institute for Cell and Molecular Bioscience, Medical School, Newcastle University, Newcastle, UK

Tóm tắt

Cyanobacterial Atx1 is a copper chaperone which interacts with two copper-transporting ATPases to assist copper supply to plastocyanin and cytochrome oxidase. ZiaA is a Zn2+-exporting ATPase and ziaA expression is regulated by ZiaR. Here we show that gene expression from the ziaA operator promoter, monitored using reverse transcriptase PCR and lacZ fusions, is elevated in Δatx1 mutants. Although Cu+ tightly binds recombinant ZiaR in vitro, Cu+ is less effective at dissociating ZiaR–DNA complexes than Zn2+ and crucially ziaA expression responds to Zn2+ but not copper in both wild-type and Δatx1 cells. Consistent with enhanced expression of ZiaA, Δatx1 cells have slightly elevated Zn2+ resistance. Recombinant Zn2+–Atx1 is recovered from Zn2+-supplemented Escherichia coli and even after copper supplementation substantial amounts of Zn2+–Atx1 are isolated. Taken together, these data suggest that Zn2+–Atx1 can form in vivo.

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