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The Pmr1 protein, the major yeast Ca2+-ATPase in the Golgi, regulates intracellular levels of the cadmium ion
被引:32
|作者:
Lauer, Claudio Marcos, Jr.
[1
,2
]
Bonatto, Diego
[3
]
Mielniczki-Pereira, Albanin Aparecida
[1
]
Schuch, Ana Zilles
[1
]
Dias, Johnny Ferraz
Yoneama, Maria-Lucia
[4
]
Henriques, Joao Antonio Pegas
[1
,3
]
机构:
[1] Univ Fed Rio Grande do Sul, Ctr Biotechnol, Dept Biofis, BR-91507970 Porto Alegre, RS, Brazil
[2] Univ Feevale, Novo Hamburgo, RS, Brazil
[3] UCS, Inst Biotechnol, Caxias Do Sul, RS, Brazil
[4] Univ Fed Rio Grande do Sul, Inst Fis, BR-91507970 Porto Alegre, RS, Brazil
关键词:
Saccharomyces cerevisiae;
Pmr1p;
secretory pathway;
Ca2+;
Mn2+-ATPases;
cadmium;
particle-induced X-ray emission;
D O I:
10.1111/j.1574-6968.2008.01214.x
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
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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页码:79 / 88
页数:10
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