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

页码：79 / 88

页数：10

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