Membrane transporters and protein traffic networks differentially affecting metal tolerance: a genomic phenotyping study in yeast

Ruotolo, Roberta; Marchini, Gessica; Ottonello, Simone

doi:10.1186/gb-2008-9-4-r67

Cited by 95 publications

(133 citation statements)

References 96 publications

(114 reference statements)

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“…To address whether more general metal/metalloid tolerance systems are involved in Te(IV) detoxification, we also compared genes revealed in this study as important for Te(IV) tolerance to genes previously reported to be important for optimal cadmium (Cd) (20,43,47,57) or arsenite [As(III)] (18,20,57) tolerance. Circumventing the issue of a generally small overlap between screens, core sets, as defined by Thorsen et al (57), corresponding to genes identified as required for resistance in at least two As(III) or two Cd screens were used.…”

Section: Sulfate Assimilation Mediates Tellurium Accumulation In Yeastmentioning

confidence: 99%

Sulfate Assimilation Mediates Tellurite Reduction and Toxicity in Saccharomyces cerevisiae

et al. 2010

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Despite a century of research and increasing environmental and human health concerns, the mechanistic basis of the toxicity of derivatives of the metalloid tellurium, Te, in particular the oxyanion tellurite, Te(IV), remains unsolved. Here, we provide an unbiased view of the mechanisms of tellurium metabolism in the yeast Saccharomyces cerevisiae by measuring deviations in Te-related traits of a complete collection of gene knockout mutants. Reduction of Te(IV) and intracellular accumulation as metallic tellurium strongly correlated with loss of cellular fitness, suggesting that Te(IV) reduction and toxicity are causally linked. The sulfate assimilation pathway upstream of Met17, in particular, the sulfite reductase and its cofactor siroheme, was shown to be central to tellurite toxicity and its reduction to elemental tellurium. Gene knockout mutants with altered Te(IV) tolerance also showed a similar deviation in tolerance to both selenite and, interestingly, selenomethionine, suggesting that the toxicity of these agents stems from a common mechanism. We also show that Te(IV) reduction and toxicity in yeast is partially mediated via a mitochondrial respiratory mechanism that does not encompass the generation of substantial oxidative stress. The results reported here represent a robust base from which to attack the mechanistic details of Te(IV) toxicity and reduction in a eukaryotic organism.

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Section: Sulfate Assimilation Mediates Tellurium Accumulation In Yeastmentioning

confidence: 99%

Sulfate Assimilation Mediates Tellurite Reduction and Toxicity in Saccharomyces cerevisiae

et al. 2010

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“…Intriguingly, the Get3 protein binds to zinc, and both its mobility on non-reducing SDS-PAGE and its subcellular localisation are affected by copper and other metals such as cobalt (Lee and Dohlman, 2008;Metz et al, 2006;Shen et al, 2003). Furthermore, the GET3 gene is strongly implicated in general metal resistance in yeast (Ruotolo et al, 2008;Schuldiner et al, 2008;Shen et al, 2003). This raises the possibility that Get3 is a multifunctional protein or, alternatively, that tail-anchored protein biogenesis can modulate cellular metal homeostasis.…”

Section: Journal Of Cell Science 122 (20)mentioning

confidence: 99%

Biogenesis of tail-anchored proteins: the beginning for the end?

Rabu

Schmid

Schwappach

et al. 2009

Journal of Cell Science

115

147

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Tail-anchored proteins are a distinct class of integral membrane proteins located in several eukaryotic organelles, where they perform a diverse range of functions. These proteins have in common the C-terminal location of their transmembrane anchor and the resulting post-translational nature of their membrane insertion, which, unlike the co-translational membrane insertion of most other proteins, is not coupled to ongoing protein synthesis. The study of tail-anchored proteins has provided a paradigm for understanding the components and pathways that mediate post-translational biogenesis of membrane proteins at the endoplasmic reticulum. In this Commentary, we review recent studies that have converged at a consensus regarding the molecular mechanisms that underlie this process – namely, that multiple pathways underlie the biogenesis of tail-anchored proteins at the endoplasmic reticulum.

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“…Cadmium enters cells through transporters evolved for the uptake of essential metals, such as iron, zinc, manganese, and calcium (7,(12)(13)(14)(15)(16). The budding yeast Saccharomyces cerevisiae has long been used as model organism to study the molecular mechanisms of cadmium toxicity and tolerance.…”

mentioning

confidence: 99%

Repression of the Low Affinity Iron Transporter Gene FET4

Caetano

Menezes

Amaral

et al. 2015

Journal of Biological Chemistry

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Background: Yap1 regulates cadmium accumulation in the vacuole and mitigates cadmium-induced ROS. Results: Yap1 induces the gene of the hypoxic repressor Rox1 that in turn represses FET4, avoiding cadmium uptake. Conclusion: Repression of FET4, via Rox1, is a novel line of defense mediated by Yap1 against cadmium toxicity. Significance: Evidence of cross-talk between oxidative and hypoxic regulators that results in increased tolerance to metal toxicity.

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Membrane transporters and protein traffic networks differentially affecting metal tolerance: a genomic phenotyping study in yeast

Cited by 95 publications

References 96 publications

Sulfate Assimilation Mediates Tellurite Reduction and Toxicity in Saccharomyces cerevisiae

Sulfate Assimilation Mediates Tellurite Reduction and Toxicity in Saccharomyces cerevisiae

Biogenesis of tail-anchored proteins: the beginning for the end?

Repression of the Low Affinity Iron Transporter Gene FET4

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