Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer

Singleton, Chloe; Brun, Nick E. Le

doi:10.1007/s10534-006-9068-1

Cited by 48 publications

(68 citation statements)

References 105 publications

(104 reference statements)

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“…As shown in Fig. 3, copper induced a conformational change in Atx1, as demonstrated by the difference between their plots and those of the DTT-treated Atx1 control; this result is in agreement with previously reported data (Singleton and Le Brun 2007). Interestingly, Cd 2?…”

Section: Resultssupporting

confidence: 92%

Cd2+ binds to Atx1 and affects the physical interaction between Atx1 and Ccc2 in Saccharomyces cerevisiae

et al. 2011

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The ATX1 deletion strain of Saccharomyces cerevisiae is more resistant to Cd(2+) than the wild-type. To investigate the function of Atx1 in Cd(2+) toxicity, we used a metal-binding assay to study the interaction between Atx1 and Cd(2+) in vitro. Using circular dichroism and two-hybrid analyses, we found that Atx1 can bind Cd(2+) specifically and that Cd(2+) binding to Atx1 affects the physical interaction between Atx1 and Ccc2. These results imply that Atx1 delivers Cd(2+) to Ccc2 and that this delivery is, at least in part, responsible for Cd(2+) toxicity in S. cerevisiae.

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Section: Resultssupporting

confidence: 92%

Cd2+ binds to Atx1 and affects the physical interaction between Atx1 and Ccc2 in Saccharomyces cerevisiae

et al. 2011

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“…On the other hand, the highly conserved region of the translated Atox1 gene in humans can be evidence for a vital role of Atox1 protein in human metabolism or embryonic development. This also might explain the still unknown phenotype of Atox1-mutation associated diseases [2] , even though different roles and regulatory factors for Atox1 in human metabolism are emerging out of recent studies [28][29][30][31] . One might speculate about a Menkes disease like phenotype resulting from a complete disruption of both functional alleles of Atox1 as suggested by Atox1 knockout mice data [32] .…”

Section: Discussionmentioning

confidence: 99%

Analysis of the human Atox 1 homologue in Wilson patients

Simon¹,

Schaefer²,

Reichert³

et al. 2008

WJG

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AIM:To analyze the metallochaperone antioxidant-1 (Atox1) gene sequence in Wilson disease patients. METHODS:Mutation analysis of the four exons of the Atox1 gene including the intron-exon boundaries was performed in 63 Wilson disease patients by direct sequencing. RESULTS:From 63 selected patients no mutations were identified after the entire coding region including the intron-exon boundaries of Atox1 were sequenced. One known polymorphism within the Atox1 gene (5'UTR -99 T>C) in 31 (49%) of the Wilson patients as well as one previously undescribed variation (5'UTR -68 C>T) in 2 of the Wilson patients could be detected. Statistical analyses revealed that the existence of a variation within the Atox1-gene showed a tendency towards an earlier onset of the disease. CONCLUSION:Based on the data of this study, no major role can be attributed to Atox1 in the pathophysiology or clinical variation of Wilson disease.

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“…The Atx1/CopZ family, probably the best characterized in this group, is responsible for cytoplasmic Cu(I) trafficking. These proteins have a characteristic MxCxxC Cu(I) binding motif and a classic βαββαβ ferredoxin-like folding [25]. In most genomes, the Cu chaperone coding gene is usually found next to a gene that encodes a P 1B -type ATPases, which drives copper efflux to the periplasmic space.…”

Section: Chaperones Oxidases and Efflux Systems To Controlmentioning

confidence: 99%

Bacterial Copper Resistance and Virulence

Pontel

Checa

Soncini

2015

Bacteria-Metal Interactions

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Copper is essential for most organisms. However, it is also toxic even at low levels, especially when its local concentration or intracellular distribution is not properly controlled. Similar to other organisms, bacteria have evolved specific copper homeostasis systems for maintaining a suitable intracellular concentration of this essential metal and at the same time, avoiding its toxic effects. Recent evidence indicates that intracellular copper actively contributes to the host innate immune response against bacterial infections and pathogens have acquired specific mechanisms to deal with this intoxicant. Here, we focus on the different arrays of metal sensing and regulatory systems employed by bacterial pathogens to mount the proper response to counteract the toxic effects of copper allowing survival and replication inside the host.

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Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer

Cited by 48 publications

References 105 publications

Cd2+ binds to Atx1 and affects the physical interaction between Atx1 and Ccc2 in Saccharomyces cerevisiae

Cd2+ binds to Atx1 and affects the physical interaction between Atx1 and Ccc2 in Saccharomyces cerevisiae

Analysis of the human Atox 1 homologue in Wilson patients

Bacterial Copper Resistance and Virulence

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