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Subcellular localization of Cd and Cd-binding peptides in tobacco leaves

Journal Article · · Plant Physiology, Supplement; (USA)
OSTI ID:6936376
;  [1]
  1. Univ. of Kentucky, Lexington (USA)

Cd-binding peptides (CdBP's) having the general structure {gamma}-(Glu-Cys){sub n}-Gly are inducible by and have high affinity for Cd. If these peptides are involved in Cd detoxification by chelation, both metal and ligand must be localized in the same cellular compartment. To address this question, we studied the vacuolar/extravacuolar distribution of Cd and CdBP's in leaves of hydroponically grown tobacco seedlings. CdBP's were induced upon addition of 20 {mu}M CdCl{sub 2} (non-phytotoxic level) to the nutrient solution. Amino acid analysis indicated that the main components were {gamma}-(Glu-Cys){sub 3}-Gly and {gamma}-(Glu-Cys){sub 4}-Gly. Purified vacuoles isolated from protoplasts of Cd treated leaves contained most of the total CdBP's and Cd found in protoplasts (104% {plus minus}8 and 110% {plus minus}8, respectively). The probability that CdBP's are synthesized extravacuolarly and their predominant location in the vacuole suggest that these molecules may be involved in translocation of Cd to the vacuole.

OSTI ID:
6936376
Journal Information:
Plant Physiology, Supplement; (USA), Journal Name: Plant Physiology, Supplement; (USA) Vol. 89:4; ISSN PPYSA; ISSN 0079-2241
Country of Publication:
United States
Language:
English