Plants and certain fungi respond to heavy metal toxicity with the indu
ced synthesis of metal-binding peptides known as phytochelatins (PCs).
With cadmium, PCs can bind the metal to form a low molecular weight P
C-Cd complex and a high molecular weight PC-Cd-S2- complex. The sulfid
e ions enhance the stability and Cd-binding capacity of the metal chel
ate, and formation of this sulfide-containing complex is associated wi
th enhanced tolerance to cadmium. Molecular analyses of two fission ye
ast mutants that fail to produce a wild type level of the PC-Cd-S2- co
mplex have determined that a vacuolar membrane transporter and several
enzymes of the purine biosynthesis pathway are necessary in vivo for
formation of the PC-Cd-S2- complex. A model based on vacuolar sequestr
ation of the PC-Cd complex by an ATP-binding cassette-type transporter
and its subsequent maturation into the stable PC-Cd-S2- complex via t
he actions of two purine biosynthetic enzymes is described.