Caenorhabditis elegans expresses a functional phytochelatin synthase.
The formation of phytochelatins, small metal-binding glutathione-derived peptides, is one of the well-studied responses of plants to toxic metal exposure. Phytochelatins have also been detected in some fungi and some marine diatoms. Genes encoding phytochelatin synthases (PCS) have recently been cloned from Arabidopsis, wheat and Schizosaccharomyces pombe. Surprisingly, database searches revealed the presence of a homologous gene in the Caenorhabditis elegans genome, DDBJ/EMBL/GenBank accession no. 266513. Here we show that C. elegans indeed expresses a gene coding for a functional phytochelatin synthase. CePCS complements the Cd2+ sensitivity of a Schizosaccharomyces pombe PCS knock-out strain and confers phytochelatin synthase activity to these cells. Thus, phytochelatins may play a role for metal homeostasis also in certain animals.
Clemens
S
S
Leibniz Institute of Plant Biochemistry, Halle, Germany. sclemens@ipb-halle.de
Schroeder
J I
JI
Degenkolb
T
T
D019881:Aminoacyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics; D002104:Cadmium / Q000494:pharmacology; D017173:Caenorhabditis elegans / Q000201:enzymology* / Q000235:genetics*; D005816:Genetic Complementation Test; D007700:Kinetics; D012568:Schizosaccharomyces / Q000187:drug effects / Q000201:enzymology / Q000235:genetics; D021241:Spectrometry, Mass, Electrospray Ionization; D014908:Triticum / Q000201:enzymology / Q000235:genetics
D002104:Cadmium; D019881:Aminoacyltransferases; C093784:glutathione gamma-glutamylcysteinyltransferase