Cd2+‐ or Hg2+‐binding proteins can replace the Cu+‐chaperone Atx1 in delivering Cu+ to the secretory pathway in yeast

Morin, Isabelle; Cuillel, Martine; Lowe, Jennifer; Crouzy, Serge; Guillain, Florent; Mintz, Elisabeth

doi:10.1016/j.febslet.2005.01.008

Cited by 13 publications

(10 citation statements)

References 41 publications

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“…3A). On the whole, Mbd1, Mbd2 and Mbd3 were less efficient than the other homologues in transferring copper to Ccc2, a feature that was not observed in our previous study [22]. Coexpression of Mbd1 or Mbd3 with Ccc2 showed a quite similar growth, in agreement with structural data obtained in vitro for the whole N-terminus of Ccc2 showing unfolded M2 [31].…”

Section: Atx1 Homologues and Copper Transfer To The Ccc2 N-terminussupporting

confidence: 88%

“…In a previous study, some structural homologues of Atx1 (namely MerP, a mercury‐binding protein from Cupriavidus metallidurans CH34 , Ntk, the MBD of the cadmium ATPase from Listeria monocytogenes , and CopZ, the metallo‐chaperone from Bacillus subtilis ), were found to be able to deliver copper to endogenous Ccc2 in an atx1Δ strain [22]. This study also showed that M1 and M2, expressed as independent proteins denoted Mbd1 and Mbd2, could also play the role of Atx1.…”

Section: Resultsmentioning

confidence: 99%

“…in copper‐ and iron‐limited media, deletion of ATX1 results in a deficient high‐affinity iron uptake and this leads to growth arrest [15]. Consequently, atx1Δ deletion strains have been used as a tool to investigate whether homologous proteins would replace Atx1 and ensure copper transport into the TGN [18–22]. Deletion of the CCC2 gene also results in a deficient high‐affinity iron uptake and leads to growth arrest in copper‐ and iron‐limited media.…”

Section: Introductionmentioning

confidence: 99%

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Dissecting the role of the N‐terminal metal‐binding domains in activating the yeast copper ATPase in vivo

et al. 2009

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In yeast, copper delivery to the trans‐Golgi network involves interactions between the metallo‐chaperone Atx1 and the N‐terminus of Ccc2, the P‐type ATPase responsible for copper transport across trans‐Golgi network membranes. Disruption of the Atx1–Ccc2 route leads to cell growth arrest in a copper‐and‐iron‐limited medium, a phenotype allowing complementation studies. Coexpression of Atx1 and Ccc2 mutants in an atx1Δccc2Δ strain allowed us to study in vivo Atx1–Ccc2 and intra‐Ccc2 domain–domain interactions, leading to active copper transfer into the trans‐Golgi network. The Ccc2 N‐terminus encloses two copper‐binding domains, M1 and M2. We show that in vivo Atx1–M1 or Atx1–M2 interactions activate Ccc2. M1 or M2, expressed in place of the metallo‐chaperone Atx1, were not as efficient as Atx1 in delivering copper to the Ccc2 N‐terminus. However, when the Ccc2 N‐terminus was truncated, these independent metal‐binding domains behaved like functional metallo‐chaperones in delivering copper to another copper‐binding site in Ccc2 whose identity is still unknown. Therefore, we provide evidence of a dual role for the Ccc2 N‐terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, thereby activating the ATPase. At variance with their prokaryotic homologues, Atx1 did not activate the Ccc2‐derived ATPase lacking its N‐terminus.

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Section: Atx1 Homologues and Copper Transfer To The Ccc2 N-terminussupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Dissecting the role of the N‐terminal metal‐binding domains in activating the yeast copper ATPase in vivo

et al. 2009

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“…The ability of ATP7B to transport metalloids other than copper has parallels to other copper efflux pumps. ATP7A is known to bind other metals such as silver (Cobine et al, 2000), and the metallochaperone Atx1 has been shown to deliver cadmium and mercury to CCC2, the ATP7B equivalent in yeast (Morin et al, 2004). It has also been reported recently that ATP7A is capable of conferring resistance to lead in astroglia in a manner that required the metal binding domains of this protein (Qian et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

Transport of Cisplatin by the Copper Efflux Transporter ATP7B

Safaei

Otani²,

Larson³

et al. 2007

Mol Pharmacol

100

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ATP7B is a P-type ATPase that mediates the efflux of copper. Recent studies have demonstrated that ATP7B regulates the cellular efflux of cisplatin (DDP) and controls sensitivity to the cytotoxic effects of this drug. To determine whether DDP is a substrate for ATP7B, DDP transport was assayed in vesicles isolated from Sf9 cells infected with a baculovirus that expressed either the wild-type ATP7B or a mutant ATP7B that was unable to transport copper as a result of conversion of the transmembrane metal binding CPC motif to CPA. Only the wild-type ATP7B-expressing vesicles exhibited copper-dependent ATPase activity, copper-induced acyl-phosphate formation, and ATP-dependent transport of copper. The amount of DDP that became bound was higher for vesicles expressing either type of ATP7B than for those not expressing either form of ATP7B, but only the vesicles expressing wild-type ATP7B mediated ATP-dependent accumulation of the drug. At pH 4.6, the vesicles expressing the wild-type ATP7B exhibited ATPdependent accumulation of DDP with an apparent K m of 1.2 Ϯ 0.5 (S.E.M.) M and V max of 0.03 Ϯ 0.002 (S.E.M.) nmol/mg of protein/min. DDP also induced the acyl-phosphorylation of ATP7B but at a much slower rate than copper. Copper and DDP each inhibited the ATP-dependent transport of the other. These results establish that DDP is a substrate for ATP7B but is transported at a much slower rate than copper.

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“…Heavy metals promote highly oxidative environments which lead to a differential level of toxicity of the metal [ 6 , 7 ]. The response to toxic elements involves diverse strategies including: redox-based metal transformation [ 8 ]; trafficking within the cytoplasm mediated by metal chaperones [ 9 , 10 ]; protein sequestration [ 11 , 12 ]; metal efflux [ 8 ]; and by metal-phosphate symport [ 13 , 14 ]. Horizontal gene transfer also plays a crucial part in the evolution of heavy metal resistance within bacterial communities [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

Survival of the Fittest: Overcoming Oxidative Stress at the Extremes of Acid, Heat and Metal

Maezato

Blum

2012

Life

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The habitat of metal respiring acidothermophilic lithoautotrophs is perhaps the most oxidizing environment yet identified. Geothermal heat, sulfuric acid and transition metals contribute both individually and synergistically under aerobic conditions to create this niche. Sulfuric acid and metals originating from sulfidic ores catalyze oxidative reactions attacking microbial cell surfaces including lipids, proteins and glycosyl groups. Sulfuric acid also promotes hydrocarbon dehydration contributing to the formation of black “burnt” carbon. Oxidative reactions leading to abstraction of electrons is further impacted by heat through an increase in the proportion of reactant molecules with sufficient energy to react. Collectively these factors and particularly those related to metals must be overcome by thermoacidophilic lithoautotrophs in order for them to survive and proliferate. The necessary mechanisms to achieve this goal are largely unknown however mechanistics insights have been gained through genomic studies. This review focuses on the specific role of metals in this extreme environment with an emphasis on resistance mechanisms in Archaea.

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Cd²⁺‐ or Hg²⁺‐binding proteins can replace the Cu⁺‐chaperone Atx1 in delivering Cu⁺ to the secretory pathway in yeast

Cited by 13 publications

References 41 publications

Dissecting the role of the N‐terminal metal‐binding domains in activating the yeast copper ATPase in vivo

Dissecting the role of the N‐terminal metal‐binding domains in activating the yeast copper ATPase in vivo

Transport of Cisplatin by the Copper Efflux Transporter ATP7B

Survival of the Fittest: Overcoming Oxidative Stress at the Extremes of Acid, Heat and Metal

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