Loss of Zhf and the tightly regulated zinc-uptake system SpZrt1 in Schizosaccharomyces pombe reveals the delicacy of cellular zinc balance.
FEMS Yeast Res
; 8(6): 883-96, 2008 Sep.
Article
em En
| MEDLINE
| ID: mdl-18637840
Abstract Zinc is an essential micronutrient, and yet it can be toxic when present in excess. Zinc acquisition and distribution are dependent on tightly controlled transport of Zn(2+) ions. Schizosaccharomyces pombe represents a second eukaryotic model to study cellular metal homeostasis. In several ways its micronutrient metabolism is fundamentally different from Saccharomyces cerevisiae. We identified the first Zn(2+)-uptake system in S. pombe and named it SpZrt1. Knock-out strains for all three ZIP (Zrt, Irt-like protein) transporters in fission yeast were constructed. Only zrt1Delta cells were unable to grow at low Zn(2+) and showed reduced (65)Zn(2+) uptake. Elemental profiles revealed a strong decrease in zinc accumulation. Cd(2+) ions inhibited uptake but Fe(2+) or Mn(2+) did not. Both mRNA abundance and protein amount are tightly regulated. Zrt1 activity is rapidly shut down upon transfer of zinc-deficient cells to zinc-replete conditions. In cells lacking Zhf, a transporter mediating endoplasmic reticulum storage of zinc, this response is about 100-fold more sensitive. Thus, removal of excess of zinc from the cytosol is largely Zhf dependent. Moreover, cells deficient for both transporters are no longer able to adjust to changing external Zn(2+) concentrations. Optimal growth is restricted to a narrow range of Zn(2+) concentrations, illustrating the fine balance between micronutrient deficiency and toxicity.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Membrana Transportadoras
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Schizosaccharomyces
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Zinco
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Regulação Fúngica da Expressão Gênica
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Proteínas de Transporte de Cátions
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Proteínas de Schizosaccharomyces pombe
Idioma:
En
Revista:
FEMS Yeast Res
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Alemanha
País de publicação:
Reino Unido