Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothioneins
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- Erwin Grill
- Lehrstuhl für Pharmazeutische Biologie, Universität München, D-8000 München 2, Federal Republic of Germany
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- Ernst-L. Winnacker
- Genzentrum der Universität München, D-8033 Martinsried, Federal Republic of Germany
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- Meinhart H. Zenk
- Lehrstuhl für Pharmazeutische Biologie, Universität München, D-8000 München 2, Federal Republic of Germany
抄録
<jats:p>Phytochelatins are a class of heavy-metal-binding peptides previously isolated from cell suspension cultures of several dicotyledonous and monocotyledonous plants. These peptides consist of repetitive γ-glutamylcysteine units with a carboxyl-terminal glycine and range from 5 to 17 amino acids in length. In the present paper we show that all plants tested synthesized phytochelatins upon exposure to heavy metal ions. No evidence for the occurrence of metallothionein-like proteins was found. All data so far obtained indicate that phytochelatins are involved in detoxification and homeostasis of heavy metals in plants and thus serve functions analogous to those of metallothioneins in animals and some fungi. Phytochelatins are induced by a wide range of metal anions and cations. Phytochelatin synthesis in suspension cultures was inhibited by buthionine sulfoximine, a specific inhibitor of γ-glutamylcysteine synthetase (EC 6.3.2.2). This finding and kinetic studies of phytochelatin induction point to a synthesis from glutathione or its precursor, γ-glutamylcysteine, in a sequential manner, thereby generating the set of homologous peptides.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 84 (2), 439-443, 1987-01
Proceedings of the National Academy of Sciences
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詳細情報 詳細情報について
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- CRID
- 1363107368783521920
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- NII論文ID
- 30016281721
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- ISSN
- 10916490
- 00278424
- http://id.crossref.org/issn/00278424
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