Reference: Lauer Junior CM, et al. (2008) The Pmr1 protein, the major yeast Ca2+-ATPase in the Golgi, regulates intracellular levels of the cadmium ion. FEMS Microbiol Lett 285(1):79-88

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Abstract

Cadmium is a nonessential, highly toxic heavy metal that shows ionic properties similar to calcium. These ionic similarities imply that the cadmium ion, Cd(2+), is a calcium ion, Ca(2+), receptor-agonist, affecting the same biochemical pathways involved in Ca(2+) homeostasis. In the yeast Saccharomyces cerevisiae, the PMC1 and PMR1 genes encode vacuolar and Golgi Ca(2+)-ATPases, respectively. The PMR1 protein product Pmr1p is involved in both Ca(2+) and Mn(2+) homeostasis. This study investigated the importance of Pmc1p and Pmr1p for Cd(2+) cellular detoxification. Using the standard techniques of yeast molecular research and a multielemental procedure named particle-induced X-ray emission, Pmr1p was identified as a protein that directly participates in the detoxification of Cd(2+), possibly through the secretory pathway. The results allow us to posit a model of Cd(2+) detoxification where Pmr1p has a central role in cell survival in a Cd(2+)-rich environment.

Reference Type
Journal Article
Authors
Lauer Junior CM, Bonatto D, Mielniczki-Pereira AA, Zilles Schuch A, Dias JF, Yoneama ML, Henriques JA
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