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AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7
Author(s) -
Abdel-Ghany Salah E.,
Burkhead Jason L.,
Gogolin Kathryn A.,
Andrés-Colás Nuria,
Bodecker Jared R.,
Puig Sergi,
Peñarrubia Lola,
Pilon Marinus
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.025
Subject(s) - chaperone (clinical) , chloroplast , yeast , organelle , dismutase , microbiology and biotechnology , copper , photosynthesis , superoxide dismutase , chemistry , biochemistry , arabidopsis thaliana , arabidopsis , atp7a , biology , gene , transporter , enzyme , medicine , organic chemistry , pathology , mutant
In plant chloroplasts two superoxide dismutase (SOD) activities occur, FeSOD and Cu/ZnSOD, with reciprocal regulation in response to copper availability. This system presents a unique model to study the regulation of metal‐cofactor delivery to an organelle. The Arabidopsis thaliana gene AtCCS encodes a functional homolog to yeast Ccs1p/Lys7p, a copper chaperone for SOD. The AtCCS protein was localized to chloroplasts where it may supply copper to the stromal Cu/ZnSOD. AtCCS mRNA expression levels are upregulated in response to Cu‐feeding and senescence. We propose that AtCCS expression is regulated to allow the most optimal use of Cu for photosynthesis.