The Pmr1 protein, the major yeast Ca2+-ATPase in the Golgi, regulates intracellular levels of the cadmium ion
Autor: | Albanin Aparecida Mielniczki-Pereira, M.L. Yoneama, Johnny Ferraz Dias, Diego Bonatto, Cláudio Marcos Lauer Júnior, Ana Zilles Schuch, João Antonio Pêgas Henriques |
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Rok vydání: | 2008 |
Předmět: |
Saccharomyces cerevisiae Proteins
ATPase Cellular detoxification Saccharomyces cerevisiae Golgi Apparatus chemistry.chemical_element Calcium-Transporting ATPases Calcium Models Biological Microbiology Plasma Membrane Calcium-Transporting ATPases symbols.namesake Genetics Molecular Biology Secretory pathway biology Golgi apparatus biology.organism_classification Yeast Cell biology Biochemistry chemistry Vacuoles biology.protein symbols Intracellular Cadmium Molecular Chaperones |
Zdroj: | FEMS Microbiology Letters. 285:79-88 |
ISSN: | 1574-6968 0378-1097 |
DOI: | 10.1111/j.1574-6968.2008.01214.x |
Popis: | 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. |
Databáze: | OpenAIRE |
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