The function of Alr1p of Saccharomyces cerevisiae in cadmium detoxification: Insights from phylogenetic studies and particle-induced X-ray emission

Kern, Ana Lúcia; Bonatto, Diego; Dias, Johnny Ferraz; Yoneama, M.L.; Brendel, Martin; Henriques, João Antônio Pêgas

doi:10.1007/s10534-004-5772-x

Cited by 13 publications

(7 citation statements)

References 39 publications

(52 reference statements)

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“…Dominant negative effects were also exerted by the mutations L750V and S795R of the mutant alleles alr1–1 and alr1–31 , which are located in the first and second TM domain, respectively. The conservative mutation from L750V is likely to affect the flexibility and integrity of a predicted hydrophobic core [21], which is presumably critical for Mg 2+ binding. The introduction of a positive charged amino acid in mutation S795R in the second TM domain is likely to alter the conformation of the transmembrane domain.…”

Section: Discussionmentioning

confidence: 99%

Oligomerization of the Mg²⁺‐transport proteins Alr1p and Alr2p in yeast plasma membrane

et al. 2006

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Alr1p is an integral plasma membrane protein essential for uptake of Mg2+ into yeast cells. Homologs of Alr1p are restricted to fungi and some protozoa. Alr1‐type proteins are distant relatives of the mitochondrial and bacterial Mg2+‐transport proteins, Mrs2p and CorA, respectively, with which they have two adjacent TM domains and a short Mg2+ signature motif in common. The yeast genome encodes a close homolog of Alr1p, named Alr2p. Both proteins are shown here to be present in the plasma membrane. Alr2p contributes poorly to Mg2+ uptake. Substitution of a single arginine with a glutamic acid residue in the loop connecting the two TM domains at the cell surface greatly improves its function. Both proteins are shown to form homo‐oligomers as well as hetero‐oligomers. Wild‐type Alr2p and mutant Alr1 proteins can have dominant‐negative effects on wild‐type Alr1p activity, presumably through oligomerization of low‐function with full‐function proteins. Chemical cross‐linking indicates the presence of Alr1 oligomers, and split‐ubiquitin assays reveal Alr1p–Alr1p, Alr2p–Alr2p, and Alr1p–Alr2p interactions. These assays also show that both the N‐terminus and C‐terminus of Alr1p and Alr2p are exposed to the inner side of the plasma membrane.

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Section: Discussionmentioning

confidence: 99%

Oligomerization of the Mg²⁺‐transport proteins Alr1p and Alr2p in yeast plasma membrane

et al. 2006

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“…ALR increases tolerance to Al 3+ and Ga 3+ ions when overexpressed in S. cerevisiae while increasing strain sensitivity to Zn 2+ , Mn 2+ , Ni 2+ , Cu 2+ , Ca 2+ , and La 3+ ions [52]. ALR proteins are also suggested to have a central role in cell survival in a cadmium-rich environment [53]. Programs for predicting TM stretches consistently predict two TM helices near the C termini of all of these proteins.…”

Section: Eukaryotic Homologuesmentioning

confidence: 97%

The CorA family: Structure and function revisited

Niegowski

Eshaghi

2007

Cell. Mol. Life Sci.

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The CorA family is a group of ion transporters that mediate transport of divalent metal ions across biological membranes. Metal ions are essential elements in most cellular processes and hence the concentrations of ions in cells and organelles must be kept at appropriate levels. Impairment of these systems is implied in a number of pathological conditions. CorA proteins are abundant among the prokaryotic organisms but homologues are present in both human and yeast. The activity of CorA proteins has generally been associated with the transport of magnesium ions but the members of the CorA family can also transport other ions such as cobalt and nickel. The structure of the CorA from Thermotoga maritima, which also was the first structure of a divalent cation transporter determined, has opened the possibilities for understanding the mechanisms behind the ion transport and also corrected a number of assumptions that have been made in the past.

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“…Alr1p, which is responsible for Mg uptake into cells, may also contribute to Cd tolerance. Mutation of the ALR1 gene results in Cd sensitivity and increased intracellular Cd levels (Kern et al, 2005), but it is not known whether Alr1p mediates Cd export. Ssu1p is a member of the major facilitator superfamily and is involved in sulphite efflux (Park & Bakalinsky, 2000).…”

Section: Other Transportersmentioning

confidence: 99%

HowSaccharomyces cerevisiaecopes with toxic metals and metalloids

2010

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Toxic metals and metalloids are widespread in nature and can locally reach fairly high concentrations. To ensure cellular protection and survival in such environments, all organisms possess systems to evade toxicity and acquire tolerance. This review provides an overview of the molecular mechanisms that contribute to metal toxicity, detoxification and tolerance acquisition in budding yeast Saccharomyces cerevisiae. We mainly focus on the metals/metalloids arsenic, cadmium, antimony, mercury, chromium and selenium, and emphasize recent findings on sensing and signalling mechanisms and on the regulation of tolerance and detoxification systems that safeguard cellular and genetic integrity.

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The function of Alr1p of Saccharomyces cerevisiae in cadmium detoxification: Insights from phylogenetic studies and particle-induced X-ray emission

Cited by 13 publications

References 39 publications

Oligomerization of the Mg²⁺‐transport proteins Alr1p and Alr2p in yeast plasma membrane

Oligomerization of the Mg²⁺‐transport proteins Alr1p and Alr2p in yeast plasma membrane

The CorA family: Structure and function revisited

HowSaccharomyces cerevisiaecopes with toxic metals and metalloids

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The function of Alr1p of Saccharomyces cerevisiae in cadmium detoxification: Insights from phylogenetic studies and particle-induced X-ray emission

Cited by 13 publications

References 39 publications

Oligomerization of the Mg2+‐transport proteins Alr1p and Alr2p in yeast plasma membrane

Oligomerization of the Mg2+‐transport proteins Alr1p and Alr2p in yeast plasma membrane

The CorA family: Structure and function revisited

HowSaccharomyces cerevisiaecopes with toxic metals and metalloids

Contact Info

Product

Resources

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Oligomerization of the Mg²⁺‐transport proteins Alr1p and Alr2p in yeast plasma membrane

Oligomerization of the Mg²⁺‐transport proteins Alr1p and Alr2p in yeast plasma membrane