Higher plants possess two different types of ATX1-like copper chaperones
Copper (Cu) chaperones constitute a family of small Cu+-binding proteins required for Cu homeostasis in eukaryotes. The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2007-03, Vol.354 (2), p.385-390 |
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| creator | Puig, Sergi Mira, Helena Dorcey, Eavan Sancenón, Vicente Andrés-Colás, Nuria Garcia-Molina, Antoni Burkhead, Jason L. Gogolin, Kathryn A. Abdel-Ghany, Salah E. Thiele, Dennis J. Ecker, Joseph R. Pilon, Marinus Peñarrubia, Lola |
| description | Copper (Cu) chaperones constitute a family of small Cu+-binding proteins required for Cu homeostasis in eukaryotes. The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidopsis cells. Interestingly, AtATX1, but not full-length CCH, interacts in vivo with the Arabidopsis RAN1 Cu-transporting P-type ATPase by yeast two-hybrid. We propose that higher plants express two types of ATX1-like Cu chaperones: the ATX1-type with a predominant function in Cu delivery to P-type ATPases, and the CCH-type with additional CTD-mediated plant-specific functions. |
| doi_str_mv | 10.1016/j.bbrc.2006.12.215 |
| format | Article |
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The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidopsis cells. Interestingly, AtATX1, but not full-length CCH, interacts in vivo with the Arabidopsis RAN1 Cu-transporting P-type ATPase by yeast two-hybrid. 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The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidopsis cells. Interestingly, AtATX1, but not full-length CCH, interacts in vivo with the Arabidopsis RAN1 Cu-transporting P-type ATPase by yeast two-hybrid. We propose that higher plants express two types of ATX1-like Cu chaperones: the ATX1-type with a predominant function in Cu delivery to P-type ATPases, and the CCH-type with additional CTD-mediated plant-specific functions.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Arabidopsis - chemistry</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - physiology</subject><subject>Copper - chemistry</subject><subject>Copper - metabolism</subject><subject>Copper chaperone</subject><subject>Copper homeostasis</subject><subject>Genome, Plant - physiology</subject><subject>Heavy metal P-type ATPase</subject><subject>Molecular Chaperones - chemistry</subject><subject>Molecular Chaperones - genetics</subject><subject>Molecular Chaperones - physiology</subject><subject>Protein Structure, Tertiary</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - physiology</subject><subject>Yeast two-hybrid</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9Lw0AQxRdRbK1-AQ-Sk7fEme3mz4KXUtQKBS8VeluSzcRuTZO4myr99m5owZtzmcO895j3Y-wWIULA5GEbFYXVEQdIIuQRx_iMjREkhBxBnLMx-EvIJa5H7Mq5LQCiSOQlG2HK-RTSbMwWC_OxIRt0dd70Luha58i5oP9pg9JUFVlq-qA_dOSCtgpmqzWGtfmkQLdd5216k_vVNuSu2UWV145uTnvC3p-fVvNFuHx7eZ3PlqEWHPpQcDFFngmQWlBexFmFMi6qWPKYUo5iGAQteYZJqrGQpcQ8xhgrnpcpwnTC7o-5nW2_9uR6tTNOU-3_p3bvVJLJFGJMvZAfhdr6UpYq1Vmzy-1BIaiBn9qqgZ8a-CnkyvPzprtT-r7YUflnOQHzgsejgHzHb0NWOW2o0VQaS7pXZWv-y_8FH65_YA</recordid><startdate>20070309</startdate><enddate>20070309</enddate><creator>Puig, Sergi</creator><creator>Mira, Helena</creator><creator>Dorcey, Eavan</creator><creator>Sancenón, Vicente</creator><creator>Andrés-Colás, Nuria</creator><creator>Garcia-Molina, Antoni</creator><creator>Burkhead, Jason L.</creator><creator>Gogolin, Kathryn A.</creator><creator>Abdel-Ghany, Salah E.</creator><creator>Thiele, Dennis J.</creator><creator>Ecker, Joseph R.</creator><creator>Pilon, Marinus</creator><creator>Peñarrubia, Lola</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20070309</creationdate><title>Higher plants possess two different types of ATX1-like copper chaperones</title><author>Puig, Sergi ; 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The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidopsis cells. Interestingly, AtATX1, but not full-length CCH, interacts in vivo with the Arabidopsis RAN1 Cu-transporting P-type ATPase by yeast two-hybrid. 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| subjects | Adenosine Triphosphatases - metabolism Arabidopsis - chemistry Arabidopsis - genetics Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - physiology Copper - chemistry Copper - metabolism Copper chaperone Copper homeostasis Genome, Plant - physiology Heavy metal P-type ATPase Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - physiology Protein Structure, Tertiary Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - physiology Yeast two-hybrid |
| title | Higher plants possess two different types of ATX1-like copper chaperones |
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