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

共 73 条

[21] NEW YEAST-ESCHERICHIA-COLI SHUTTLE VECTORS CONSTRUCTED WITH INVITRO MUTAGENIZED YEAST GENES LACKING 6-BASE PAIR RESTRICTION SITES [J].

GIETZ, RD ;

SUGINO, A .

GENE, 1988, 74 (02) :527-534

[22] Toxic and essential metal interactions [J].

Goyer, RA .

ANNUAL REVIEW OF NUTRITION, 1997, 17 :37-50

[23]

Greger R., 1996, P2427

[24] Elevated cytosolic free Ca2+ concentrations and massive Ca2+ accumulation within vacuoles, in yeast mutant lacking PMR1, a homolog of Ca2+-ATPase [J].

Halachmi, D ;

Eilam, Y .

FEBS LETTERS, 1996, 392 (02) :194-200

[25] Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease [J].

Hu, ZL ;

Bonifas, JM ;

Beech, J ;

Bench, G ;

Shigihara, T ;

Ogawa, H ;

Ikeda, S ;

Mauro, T ;

Epstein, EH .

NATURE GENETICS, 2000, 24 (01) :61-65

[26] Integration of stress responses:: Modulation of calcineurin signaling in Saccharomyces cerevisiae by protein kinase A [J].

Kafadar, KA ;

Cyert, MS .

EUKARYOTIC CELL, 2004, 3 (05) :1147-1153

[27]

KATHRYN JM, 2004, DIABETES, V253, P393

[28] Cadmium, osteoporosis and calcium metabolism [J].

Kazantzis, G .

BIOMETALS, 2004, 17 (05) :493-498

[29] Hailey-Halley disease as an orthodisease of PMR1 deficiency in Saccharomyees cerevisiae [J].

Kellermayer, R .

FEBS LETTERS, 2005, 579 (10) :2021-2025

[30] Extracellular Ca2+ sensing contributes to excess Ca2+ accumulation and vacuolar fragmentation in a pmr1Δ mutant of S-cerevisiae [J].

Kellermayer, R ;

Aiello, DP ;

Miseta, A ;

Bedwell, DM .

JOURNAL OF CELL SCIENCE, 2003, 116 (08) :1637-1646

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