Abstract
Exposure of several species of the family Poaceae to cadmium results in the formation of metal-induced peptides of the general structure (gamma-Glu-Cys)n-Ser (n=2-4). They are assumed to be formed from hydroxymethyl-glutathione (gamma-Glu-Cys-Ser) and are termed hydroxymethyl-phytochelatins (hm-PCs) in analogy to the homo-phytochelatins [(gamma-Glu-Cys)n-beta-Ala], discovered in legumes, and the phytochelatins [PCs, (gamma-Glu-Cys)n-Gly] found in most other plants and many fungi. The hm-PCs were isolated from the roots of cadmium-exposed rice (Oryza sativa L. cv Strella), and their structure was confirmed by amino acid analysis after total and enzymic hydrolysis and by tandem mass spectrometry. The hm-PCs probably play a significant role in heavy metal detoxication in rice. In addition to this new form of gamma-Glu-Cys (gamma EC) peptide, PCs and gamma EC peptides without C-terminal Ser or Gly are found. All gamma EC peptides are synthesized without delay after incubation of rice plants in 100 microM CdCl2 in the roots as well as in the shoots. Incubation times exceeding 24 h or higher concentrations of cadmium result in a selective enrichment of gamma EC peptides with higher chain length and an increased ratio of PCs to hm-PCs. gamma EC peptide synthesis is accompanied by a decrease of the glutathione content and an increase of the hydroxymethyl-glutathione content in roots and shoots of rice plants.
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Selected References
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- Barbas J., Santhanagopalan V., Blaszczynski M., Ellis W. R., Jr, Winge D. R. Conversion in the peptides coating cadmium:sulfide crystallites in Candida glabrata. J Inorg Biochem. 1992 Nov 1;48(2):95–105. doi: 10.1016/0162-0134(92)80019-r. [DOI] [PubMed] [Google Scholar]
- Grill E., Löffler S., Winnacker E. L., Zenk M. H. Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase). Proc Natl Acad Sci U S A. 1989 Sep;86(18):6838–6842. doi: 10.1073/pnas.86.18.6838. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grill E., Winnacker E. L., Zenk M. H. Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothioneins. Proc Natl Acad Sci U S A. 1987 Jan;84(2):439–443. doi: 10.1073/pnas.84.2.439. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hayashi Y., Nakagawa C. W., Mutoh N., Isobe M., Goto T. Two pathways in the biosynthesis of cadystins (gamma EC)nG in the cell-free system of the fission yeast. Biochem Cell Biol. 1991 Feb-Mar;69(2-3):115–121. doi: 10.1139/o91-018. [DOI] [PubMed] [Google Scholar]
- Isobe M., Uyakul D., Liu K. L., Goto T. FAB-MS/MS spectrometry in determining the primary structure of gamma-glutamyl-containing peptides. Agric Biol Chem. 1990 Jul;54(7):1651–1660. [PubMed] [Google Scholar]
- Kneer R., Kutchan T. M., Hochberger A., Zenk M. H. Saccharomyces cerevisiae and Neurospora crassa contain heavy metal sequestering phytochelatin. Arch Microbiol. 1992;157(4):305–310. doi: 10.1007/BF00248673. [DOI] [PubMed] [Google Scholar]
- Kägi J. H., Kojima Y. Chemistry and biochemistry of metallothionein. Experientia Suppl. 1987;52:25–61. doi: 10.1007/978-3-0348-6784-9_3. [DOI] [PubMed] [Google Scholar]
- Rauser W. E. Phytochelatins. Annu Rev Biochem. 1990;59:61–86. doi: 10.1146/annurev.bi.59.070190.000425. [DOI] [PubMed] [Google Scholar]
- Reese R. N., Mehra R. K., Tarbet E. B., Winge D. R. Studies on the gamma-glutamyl Cu-binding peptide from Schizosaccharomyces pombe. J Biol Chem. 1988 Mar 25;263(9):4186–4192. [PubMed] [Google Scholar]
- Reese R. N., Winge D. R. Sulfide stabilization of the cadmium-gamma-glutamyl peptide complex of Schizosaccharomyces pombe. J Biol Chem. 1988 Sep 15;263(26):12832–12835. [PubMed] [Google Scholar]
- Roepstorff P., Fohlman J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed Mass Spectrom. 1984 Nov;11(11):601–601. doi: 10.1002/bms.1200111109. [DOI] [PubMed] [Google Scholar]
