The MXCXXC class of metallochaperone proteins: model studies

Shoshan, Michal S.; Tshuva, Edit Y.

doi:10.1039/c1cs15086c

Cited by 17 publications

(16 citation statements)

References 76 publications

(99 reference statements)

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“…7 Here, we found that overexpression of ATX1 resulted in hypersensitivity to severe Cu deficiency. By contrast, overexpression of mutated ATX1 did not show the hypersensitivity.…”

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confidence: 86%

Overexpression of ArabidopsisATX1retards plant growth under severe copper deficiency

Shin

Yeh

2012

Plant Signaling & Behavior

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“…7 Here, we found that overexpression of ATX1 resulted in hypersensitivity to severe Cu deficiency. By contrast, overexpression of mutated ATX1 did not show the hypersensitivity.…”

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confidence: 86%

Overexpression of ArabidopsisATX1retards plant growth under severe copper deficiency

Shin

Yeh

2012

Plant Signaling & Behavior

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“…As a Cu chaperone, ATX1 cannot directly transport Cu across membranes, but it may deliver Cu to the target proteins for Cu trafficking. Yeast ATX1 and AtATX1 in Arabidopsis have been reported to chelate Cu in the binding site containing the MXCXXC conserved sequence (Pufahl et al, 1997;Shoshan and Tshuva, 2011;, which is important for Cudependent protein-protein interaction (Pufahl et al, 1997;Andrés-Colás et al, 2006;Puig et al, 2007;Shoshan and Tshuva, 2011;. The alignment of protein sequences revealed that OsATX1 contains an MXCXXC Cu + -binding motif (Supplemental Fig.…”

Section: Osatx1 Affects Cu Transport and Distribution Probably By Intmentioning

confidence: 99%

OsATX1 Interacts with Heavy Metal P1B-Type ATPases and Affects Copper Transport and Distribution

et al. 2018

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Copper (Cu) is an essential micronutrient for plant growth. However, the molecular mechanisms underlying Cu trafficking and distribution to different organs in rice () are poorly understood. Here, we report the function and role of Antioxidant Protein1 (OsATX1), a Cu chaperone in rice. Knocking out resulted in increased Cu concentrations in roots, whereas overexpression reduced root Cu concentrations but increased Cu accumulation in the shoots. At the reproductive stage, the concentrations of Cu in developing tissues, including panicles, upper nodes and internodes, younger leaf blades, and leaf sheaths of the main tiller, were increased significantly in -overexpressing plants and decreased in mutants compared with the wild type. The mutants also showed a higher Cu concentration in older leaves. Yeast two-hybrid and bimolecular fluorescence complementation assays showed that OsATX1 interacts with the rice heavy metal P-ATPases HMA4, HMA5, HMA6, and HMA9. These results suggest that OsATX1 may function to deliver Cu to heavy metal P-ATPases for Cu trafficking and distribution in order to maintain Cu homeostasis in different rice tissues. In addition, heterologous expression of in the yeast () cadmium-sensitive mutant Δ increased the tolerance to Cu and cadmium by decreasing their respective concentrations in the transformed yeast cells. Taken together, our results indicate that OsATX1 plays an important role in facilitating root-to-shoot Cu translocation and the redistribution of Cu from old leaves to developing tissues and seeds in rice.

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“…Yeast ATX1 was reported to chelate Cu with excellent affinity (Pufahl et al, 1997;Shoshan and Tshuva, 2011). Additionally, the MXCXXC motif of yeast ATX1 acts as a high-affinity Cu-binding site and is important for Cu-dependent protein-protein interaction (Pufahl et al, 1997;Shoshan and Tshuva, 2011).…”

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confidence: 99%

“…Additionally, the MXCXXC motif of yeast ATX1 acts as a high-affinity Cu-binding site and is important for Cu-dependent protein-protein interaction (Pufahl et al, 1997;Shoshan and Tshuva, 2011). The alignment of protein sequences revealed that ATX1 in Arabidopsis contains only one MXCXXC motif and the only known metal-binding motif (Supplemental Fig.…”

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confidence: 99%

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Copper Chaperone Antioxidant Protein1 Is Essential for Copper Homeostasis

2012

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Copper (Cu) is essential for plant growth but toxic in excess. Specific molecular mechanisms maintain Cu homeostasis to facilitate its use and avoid the toxicity. Cu chaperones, proteins containing a Cu-binding domain(s), are thought to assist Cu intracellular homeostasis by their Cu-chelating ability. In Arabidopsis (Arabidopsis thaliana), two Cu chaperones, Antioxidant Protein1 (ATX1) and ATX1-Like Copper Chaperone (CCH), share high sequence homology. Previously, their Cu-binding capabilities were demonstrated and interacting molecules were identified. To understand the physiological functions of these two chaperones, we characterized the phenotype of atx1 and cch mutants and the cchatx1 double mutant in Arabidopsis. The shoot and root growth of atx1 and cchatx1 but not cch was specifically hypersensitive to excess Cu but not excess iron, zinc, or cadmium. The activities of antioxidant enzymes in atx1 and cchatx1 were markedly regulated in response to excess Cu, which confirms the phenotype of Cu hypersensitivity. Interestingly, atx1 and cchatx1 were sensitive to Cu deficiency. Overexpression of ATX1 not only enhanced Cu tolerance and accumulation in excess Cu conditions but also tolerance to Cu deficiency. In addition, the Cu-binding motif MXCXXC of ATX1 was required for these physiological functions. ATX1 was previously proposed to be involved in Cu homeostasis by its Cu-binding activity and interaction with the Cu transporter Heavy metal-transporting P-type ATPase5. In this study, we demonstrate that ATX1 plays an essential role in Cu homeostasis in conferring tolerance to excess Cu and Cu deficiency. The possible mechanism is discussed.

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The MXCXXC class of metallochaperone proteins: model studies

Cited by 17 publications

References 76 publications

Overexpression of ArabidopsisATX1retards plant growth under severe copper deficiency

Overexpression of ArabidopsisATX1retards plant growth under severe copper deficiency

OsATX1 Interacts with Heavy Metal P1B-Type ATPases and Affects Copper Transport and Distribution

Copper Chaperone Antioxidant Protein1 Is Essential for Copper Homeostasis

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