Copper chaperones in Arabidopsis thaliana. Intra cellular copper trafficking: uptake, delivery and regulation
Date
2004
Authors
Bodecker, Jared, author
Abdel-Ghany, Salah E., author
Burkhead, Jason, author
Pilon, Marinus, author
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Abstract
The chloroplast is the site of photosynthesis. Copper is an essential element to chloroplast function as a co-factor of superoxide dismutase (SOD) and plastocyanin, which function in photosynthesis. Chloroplasts have a complex structure due to the presence of three membranes, so how then is Copper delivered throughout the complex internal structure of plant chloroplasts? In plant chloroplasts, membrane transporters have been identified that transport Copper across these membranes. In microbes, a family of small cytoplasmic proteins called 1cmetallochaperones 1d or Copper Chaperones carries out the delivery of copper from transporters to targets. After these chaperones bind to copper, they deliver and insert the copper ions into an active site of a specific partner, a copper dependent enzyme or another transporter. In the genome of A. thaliana possible genes encoding for copper chaperones have been identified based on the similarity of sequences with microbial chaperones. We named these, CpCCS (Chloroplastic Copper Chaperone for SOD1), ATX2 (similar to yeast Antioxidant protein) and CpCopZ. These three A. thaliana Cu Chaperone proteins may be required for Cu transport to the internal compartments of the chloroplast. To test the function of the putative copper chaperones in copper delivery two approaches are taken. First we test complementation of yeast mutants, deficient in copper chaperones. Second, we analyze the function and need for these proteins in plants with the insertions (KO-mutants) in each copper chaperone gene.
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Subject
Plants -- Effect of copper on
Chloroplasts
Plant proteins
Arabidopsis thaliana