Arabidopsis copper chaperone (CCH) belongs to a family of eukaryotic protei
ns 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 petiol
es, as shown by tissue prints and immunohistochemical detection. CCH protei
n also accumulates in stem sieve elements and is collected in phloem exudat
es. Accordingly, Arabidopsis CCH is the only member of the metallochaperone
family described to function intercellularly to date. Moreover, the CCH pr
otein 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 struc
tures, as a result of metalloprotein breakdown.