Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae

Phytochelatins (PCs) are cysteine-rich peptides that chelate heavy metal ions, thereby mediating heavy metal tolerance in plants, fission yeast, and Caenorhabditis elegans. They are synthesized from glutathione by PC synthase, a specific dipeptidyltransferase. While Saccharomyces cerevisiae synthesi...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 2007-04, Vol.581 (8), p.1681-1687
Main Authors: Wünschmann, Jana, Beck, Andreas, Meyer, Laurent, Letzel, Thomas, Grill, Erwin, Lendzian, Klaus J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Caenorhabditis elegans
Carboxypeptidase C
Carboxypeptidase Y
Carboxypeptidases - genetics
Carboxypeptidases - metabolism
Glutathione
Glutathione - biosynthesis
Glutathione - genetics
Metal tolerance
Molecular Sequence Data
Phytochelatins
S. cerevisiae
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Schizosaccharomyces pombe
Vacuoles - enzymology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Phytochelatins (PCs) are cysteine-rich peptides that chelate heavy metal ions, thereby mediating heavy metal tolerance in plants, fission yeast, and Caenorhabditis elegans. They are synthesized from glutathione by PC synthase, a specific dipeptidyltransferase. While Saccharomyces cerevisiae synthesizes PCs upon exposure to heavy metal ions, the S. cerevisiae genome does not encode a PC synthase homologue. How PCs are synthesized in yeast is unclear. This study shows that the vacuolar serine carboxypeptidases CPY and CPC are responsible for PC synthesis in yeast. The finding of a PCS-like activity of these enzymes in vivo discloses another route for PC biosynthesis in eukaryotes.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.03.039