4.8 Article

Evidence for the plant-specific intercellular transport of the Arabidopsis copper chaperone CCH

Journal

PLANT JOURNAL
Volume 25, Issue 5, Pages 521-528

Publisher

BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1365-313x.2001.00985.x

Keywords

ATX1-homologue; CCH; copper homeostasis; metallochaperone; phloem transport; senescence

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Arabidopsis copper chaperone (CCH) belongs to a family of eukaryotic proteins that participates in intracellular copper homeostasis by delivering this metal to the secretory pathway. In this work we show that the CCH protein is mainly located along the vascular bundles of senescing leaves and petioles, as shown by tissue prints and immunohistochemical detection. CCH protein also accumulates in stem sieve elements and is collected in phloem exudates. Accordingly, Arabidopsis CCH is the only member of the metallochaperone family described to function intercellularly to date. Moreover, the CCH protein remains stable when plants are subjected to excess copper that causes a rapid and specific decrease in its mRNA. These facts point to a role for CCH in copper mobilization from decaying organs towards reproductive structures, as a result of metalloprotein breakdown.

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