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Spoils of war: iron at the crux of clinical and ecological fitness of Pseudomonas aeruginosa

Acyl peptidic siderophores: structures, biosyntheses and post-assembly modifications

The fate of siderophores: antagonistic environmental interactions in exudate-mediated micronutrient uptake

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Manganese uptake and streptococcal virulence

Host-imposed manganese starvation of invading pathogens: two routes to the same destination

Wounding of Arabidopsis halleri leaves enhances cadmium accumulation that acts as a defense against herbivory

Speciation of uranium in compartments of living cells

Siderophore–fluoroquinolone conjugates containing potential reduction-triggered linkers for drug release: synthesis and antibacterial activity

Synthesis, characterization and biological activity of Cu(II), Zn(II) and Re(I) complexes derived from S-benzyldithiocarbazate and 3-acetylcoumarin

Iron loading site on the Fe–S cluster assembly scaffold protein is distinct from the active site

Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro

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Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro

Content Provider	Springer Nature Link
Author	Petzoldt, Svenja Kahra, Dana Kovermann, Michael Dingeldein, Artur PG Niemiec, Moritz S. Ådén, Jörgen Wittung Stafshede, Pernilla
Copyright Year	2015
Abstract	After Ctr1-mediated copper ion (Cu) entry into the human cytoplasm, chaperones Atox1 and CCS deliver Cu to P1B-type ATPases and to superoxide dismutase, respectively, via direct protein–protein interactions. Although the two Cu chaperones are presumed to work along independent pathways, we here assessed cross-reactivity between Atox1 and the first domain of CCS (CCS1) using biochemical and biophysical methods in vitro. By NMR we show that CCS1 is monomeric although it elutes differently from Atox1 in size exclusion chromatography (SEC). This property allows separation of Atox1 and CCS1 by SEC and, combined with the 254/280 nm ratio as an indicator of Cu loading, we demonstrate that Cu can be transferred from one protein to the other. Cu exchange also occurs with full-length CCS and, as expected, the interaction involves the metal binding sites since mutation of Cu-binding cysteine in Atox1 eliminates Cu transfer from CCS1. Cross-reactivity between CCS and Atox1 may aid in regulation of Cu distribution in the cytoplasm.
Starting Page	577
Ending Page	585
Page Count	9
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	28
Issue Number	3
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2015-02-12
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Human copper transport Atox1 Copper chaperone for superoxide dismutase (SOD) Size exclusion chromatography Proton-NMR Biochemistry Pharmacology/Toxicology Microbiology Cell Biology Plant Physiology Medicine/Public Health
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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Multiple Protein Domains Contribute to the Action of the Copper Chaperone for Superoxide Dismutase

Roles of copper chaperone for superoxide dismutase 1 and metallothionein in copper homeostasis

Copper transporters and chaperones CTR1, CTR2, ATOX1, and CCS as determinants of cisplatin sensitivity

Copper–zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1

Mechanism of Cu,Zn-Superoxide Dismutase Activation by the Human Metallochaperone hCCS

Changes in copper concentrations affect the protein levels but not the mRNA levels of copper chaperones in human umbilical vein endothelial cells

Distorted copper homeostasis with decreased sensitivity to cisplatin upon chaperone Atox1 deletion in Drosophila

Characteristics of copper tolerance in Yarrowia lipolytica

Models for the mechanism for activating copper-zinc superoxide dismutase in the absence of the CCS Cu chaperone in Arabidopsis

Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro

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Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro