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
来源：
FEMS MICROBIOLOGY LETTERS | 2008年 / 285卷 / 01期
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.
引用
收藏
页码：79 / 88
页数：10
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