Difference between revisions of "Phytochelatin"
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Phytochelatins are oligomers of glutathione, produced by the enzyme phytochelatin synthase. They are found in plants, fungi, nematodes and all groups of algae including cyanobacteria. Phytochelatins act as chelators, and are important for heavy metal detoxification.[1][2][3] They are abbreviated PC2 through PC11.
A mutant Arabidopsis thaliana lacking phytochelatin synthase is very sensitive to cadmium, but it grows just as well as the wild-type plant at normal concentrations of zinc and copper, two essential metal ions, indicating that phytochelatin is only involved in resistance to metal poisoning.[4]
Because phytochelatin synthase uses glutathione with a blocked thiol group in the synthesis of phytochelatin, the presence of heavy metal ions that bind to glutathione causes the enzyme to work faster. Therefore the amount of phytochelatin increases when the cell needs more phytochelatin to survive in an environment with high concentrations of metal ions.[5]
Phytochelatin seems to be transported into the vacuole of plants, so that the metal ions it carries are stored safely away from the proteins of the cytosol.[4]
Related peptides
There are groups of other peptides with a similar structure to phytochelatin, but where the last amino acid is not glycine:[4][6]
| Type | Structure | Has been found in | Precursor |
|---|---|---|---|
| Phytochelatin | (γGlu-Cys)n-Gly | many organisms | Glutathione |
| Homophytochelatin | (γGlu-Cys)n-Ala | legumes | Homoglutathione |
| Desglycine phytochelatin | (γGlu-Cys)n | maize, yeasts | |
| Hydroxymethyl-phytochelatin | (γGlu-Cys)n-Ser | grasses | Hydroxymethylglutathione |
| iso-Phytochelatin (Glu) | (γGlu-Cys)n-Glu | maize | Glutamylcysteinylglutamate |
| iso-Phytochelatin (Gln) | (γGlu-Cys)n-Gln | horseradish |
History
Phytochelatin was first discovered in 1981 in fission yeast,[7][8] and was named cadystin.[9] It was then found in higher plants in 1985 and was named phytochelatin. In 1989 its enzyme, phytochelatin synthase, was discovered.[6]
See also
References
- ↑ Suk-Bong Ha, Aaron P. Smith, Ross Howden, Wendy M. Dietrich, Sarah Bugg, Matthew J. O'Connell, Peter B. Goldsbrough, and Christopher S. Cobbett (1999). "Phytochelatin Synthase Genes from Arabidopsis and the Yeast Schizosaccharomyces pombe". Plant Cell. 11 (6): 1153–1164. doi:10.1105/tpc.11.6.1153. PMC 144235 Freely accessible. PMID 10368185.
- ↑ Olena K. Vatamaniuk, Elizabeth A. Bucher, James T. Ward and Philip A. Rea (2001). "A new pathway for heavy metal detoxification in animals: phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans". J. Biol. Chem. 276 (24): 20817. doi:10.1074/jbc.C100152200. PMID 11313333.
- ↑ InterPro database page on phytochelatin synthase
- ↑ 4.0 4.1 4.2 Buchanan, Gruissem, Jones, Biochemistry & molecular biology of plants, 1st edition, American Society of Plant Physiology, 2000
- ↑ O K Vatamaniuk, S Mari, Y Lu, and P A Rea (2000). "Mechanism of Heavy Metal Ion Activation of Phytochelatin (PC) Synthase". J. Biol. Chem. 275 (40): 31451–31459. doi:10.1074/jbc.M002997200. PMID 10807919.
- ↑ 6.0 6.1 Masahiro Inouhe (2005). "Phytochelatins". Brazilian Journal of Plant Physiology. 17. doi:10.1590/S1677-04202005000100006.
- ↑ Akira Murasugi, Chiaki Wada, and Yukimasa Hayashi (1981). "Cadmium-Binding Peptide Induced in Fission Yeast, Schizosaccharomyces pombe". J. Biochem. 90, 1561-1564. PMID 7338524.
- ↑ Akira Murasugi, Chiaki Wada, and Yukimasa Hayashi (1981). "Purification and Unique Properties in UV and CD Spectra of Cd-Binding Peptide 1 from Scizosaccharomyces pombe". Biochem. Biophys. Res. Commun. 103 1021-1028. PMID 7332570.
- ↑ Naoto Kondo, Kunio Imai, Minoru Isobe, Toshio Goto, Akira Murasugi, Chiaki Wada-Nakagawa, Yukimasa Hayashi (1984)."Cadystin A and B, Major Unit Peptides Comprising Cadmium Binding Peptides Induced in a Fission Yeast----Separation, Revision of Structures and Synthesis". Tetrahedron Lett. 25 3869-3872. doi: 10.1016/S0040-4039(01)91190-6.
