The Pmr1 protein, the major yeast Ca2+-ATPase in the Golgi, regulates intracellular levels of the cadmium ion |
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| Authors: | Lauer Júnior Cláudio Marcos Bonatto Diego Mielniczki-Pereira Albanin Aparecida Schuch Ana Zilles Dias Johnny Ferraz Yoneama Maria-Lúcia Pêgas Henriques João Antonio |
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| Affiliation: | Departamento de Biofísica/Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil;;Universitário Feevale, Campus II, Novo Hamburgo, RS, Brazil;;Instituto de Biotecnologia, Universidade de Caxias do Sul (UCS), Bloco, Caxias do Sul, RS, Brazil;and;Instituto de Física, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil |
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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, Cd2+, is a calcium ion, Ca2+, receptor-agonist, affecting the same biochemical pathways involved in Ca2+ homeostasis. In the yeast Saccharomyces cerevisiae , the PMC1 and PMR1 genes encode vacuolar and Golgi Ca2+-ATPases, respectively. The PMR1 protein product Pmr1p is involved in both Ca2+ and Mn2+ homeostasis. This study investigated the importance of Pmc1p and Pmr1p for Cd2+ 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 Cd2+, possibly through the secretory pathway. The results allow us to posit a model of Cd2+ detoxification where Pmr1p has a central role in cell survival in a Cd2+-rich environment. |
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| Keywords: | Saccharomyces cerevisiae Pmr1p secretory pathway Ca2+/Mn2+-ATPases cadmium particle-induced X-ray emission |
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