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Gene Review:

pcs-1 - Protein PCS-1

Caenorhabditis elegans

Wysocki, R. et al., Harada, E. et al., Vatamaniuk, O.K. et al., Vatamaniuk, O.K. et al.

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High impact information on pcs-1

A new pathway for heavy metal detoxification in animals. Phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans [1].
Phytochelatin synthase is the enzyme responsible for the synthesis of heavy-metal-binding peptides (phytochelatins) from glutathione and related thiols [2].
On the other hand, we show for the first time that phytochelatins also contribute to antimony tolerance as PCS fully complement antimonite sensitivity of ycf1Delta mutant [3].
The S. pombe and wheat phytochelatin synthase (PCS) genes, when expressed in S. cerevisiae, mediate only modest resistance to arsenite and thus cannot functionally compensate for Acr3p [3].
A cyanobacterial protein with similarity to phytochelatin synthases catalyzes the conversion of glutathione to gamma-glutamylcysteine and lacks phytochelatin synthase activity [4].

References

A new pathway for heavy metal detoxification in animals. Phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans. Vatamaniuk, O.K., Bucher, E.A., Ward, J.T., Rea, P.A. J. Biol. Chem. (2001) [Pubmed]
Worms take the 'phyto' out of 'phytochelatins'. Vatamaniuk, O.K., Bucher, E.A., Ward, J.T., Rea, P.A. Trends Biotechnol. (2002) [Pubmed]
Metalloid tolerance based on phytochelatins is not functionally equivalent to the arsenite transporter Acr3p. Wysocki, R., Clemens, S., Augustyniak, D., Golik, P., Maciaszczyk, E., Tamás, M.J., Dziadkowiec, D. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
A cyanobacterial protein with similarity to phytochelatin synthases catalyzes the conversion of glutathione to gamma-glutamylcysteine and lacks phytochelatin synthase activity. Harada, E., von Roepenack-Lahaye, E., Clemens, S. Phytochemistry (2004) [Pubmed]

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