Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance

Delhaize, Emmanuel; Kataoka, Takahito; Hebb, Diane M.; White, Rosemary G.; Ryan, Peter R.

doi:10.1105/tpc.009134

Cited by 228 publications

(233 citation statements)

References 51 publications

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“…This is similar to the Stylosanthes hamata metal tolerance protein ShMtp1's case. This protein is a member of CDF transporter family, and detoxifies manganese in this plant (Delhaize et al, 2003). ShMtp1 shares high sequence similarity with Arabidopsis and rice CDF proteins, but only ShMtp1 protein has manganese detoxification activity which is parallel to our results with NIC6.…”

Section: Discussionsupporting

confidence: 85%

Characterization of a cDNA from Beta maritima that confers nickel tolerance in yeast

Bozdag

Kaya

Koç

et al. 2014

Gene

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Nickel is an essential micronutrient due to its involvement in many enzymatic reactions as a cofactor. However, excess of this element is toxic to biological systems. Here, we constructed a cDNA library from Beta maritima and screened it in the yeast system to identify genes that confer resistance to toxic levels of nickel. A cDNA clone (NIC6), which encodes for a putative membrane protein with unknown function, was found to help yeast cells to tolerate toxic levels of nickel. A GFP fused form of Nic6 protein was localized to multivesicular structures in tobacco epidermal cells. Thus, our results suggest a possible role of Nic6 in nickel and intracellular ion homeostasis.

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Section: Discussionsupporting

confidence: 85%

Characterization of a cDNA from Beta maritima that confers nickel tolerance in yeast

Bozdag

Kaya

Koç

et al. 2014

Gene

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“…The second vacuolar Mn transporter, ShMTP1, is a member of the cation diffusion facilitator (CDF) family of heavy metal transporters and was cloned from the highly Mn-tolerant plant Stylosanthes hamata (13). This protein increased Mn tolerance and accumulation when expressed in yeast or Arabidopsis (13).…”

mentioning

confidence: 99%

“…Plants that tolerate high Mn concentrations can exhibit distinct compartmentation patterns, such as accumulation in the epidermal cell layer (9) and deposition in trichomes (10). In conditions of high Mn supply, plants accumulate high concentrations of the metal in vacuoles (11) and ectopic expression of vacuolar Mn transporters can increase the Mn tolerance of plants (12,13).…”

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confidence: 99%

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A secretory pathway-localized cation diffusion facilitator confers plant manganese tolerance

Peiter

Montanini

Gobert

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

253

262

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Manganese toxicity is a major problem for plant growth in acidic soils, but cellular mechanisms that facilitate growth in such conditions have not been clearly delineated. Established mechanisms that counter metal toxicity in plants involve chelation and cytoplasmic export of the metal across the plasma or vacuolar membranes out of the cell or sequestered into a large organelle, respectively. We report here that expression of the Arabidopsis and poplar MTP11 cation diffusion facilitators in a manganesehypersensitive yeast mutant restores manganese tolerance to wild-type levels. Microsomes from yeast expressing AtMTP11 exhibit enhanced manganese uptake. In accord with a presumed function of MTP11 in manganese tolerance, Arabidopsis mtp11 mutants are hypersensitive to elevated levels of manganese, whereas plants overexpressing MTP11 are hypertolerant. In contrast, sensitivity to manganese deficiency is slightly decreased in mutants and increased in overexpressing lines. Promoter-GUS studies showed that AtMTP11 is most highly expressed in root tips, shoot margins, and hydathodes, but not in epidermal cells and trichomes, which are generally associated with manganese accumulation. Surprisingly, imaging of MTP11-EYFP fusions demonstrated that MTP11 localizes neither to the plasma membrane nor to the vacuole, but to a punctate endomembrane compartment that largely coincides with the distribution of the trans-Golgi marker sialyl transferase. Golgi-based manganese accumulation might therefore result in manganese tolerance through vesicular trafficking and exocytosis. In accord with this proposal, Arabidopsis mtp11 mutants exhibit enhanced manganese concentrations in shoots and roots. We propose that Golgi-mediated exocytosis comprises a conserved mechanism for heavy metal tolerance in plants.Golgi ͉ heavy metal transport ͉ metal tolerance protein ͉ metal trafficking ͉ manganese transporter T ransition metals are required by living systems where they perform a wide variety of functions as cofactors for enzymes and transcription factors. Transition metals are also present in many environments at potentially toxic concentrations, and this has led to the evolution of mechanisms that counter toxicity. In plants exposed to high concentrations of transition metals in the soil, binding of the metals to phytochelatins in the cytosol lowers metal activity (1). Additionally, metals can be removed from the cytosol through the action of metal transporters. Transporters involved in metal tolerance localize to the plasma membrane, thereby removing metals from the cell, or to the vacuolar membrane, where the metal can be sequestered into a large and metabolically relatively inert intracellular compartment (2).Manganese is the second most prevalent transition metal, after iron, in the Earth's crust and an essential micronutrient for all organisms, including humans and plants (3). In addition to being a cofactor for a variety of enzymes (including various decarboxylases of the tricarboxylic acid cycle, RNA polymerases, and numerous glyco...

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“…Several mechanisms of Mn tolerance have been proposed: (1) sequestration of Mn in the apoplast thus preventing Mn oxidation (Maier, 1997;, (2) transport of Mn into the vacuoles (Hirschi et al, 2000;Schaaf et al, 2002;Delhaize et al, 2003) and sequestration by organic acids (Maier, 1997;, (3) maintaining low cytosolic Mn concentrations by enhanced transport of Mn into the endoplasmic reticulum (Wu et al, 2002), and (4) scavenging the Mninduced enhanced formation of reactive oxygen species (ROS), phenoxy radicals, and Mn III by an efficient ascorbic acid turnover in the apoplast and cytoplasm (Fecht-Christoffers et al, 2003b;Fecht-Christoffers and Horst, 2005). But so far, none of the factors can satisfactorily explain genotypically enhanced Mn tolerance in cowpea .…”

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confidence: 99%

The Role of Hydrogen Peroxide-Producing and Hydrogen Peroxide-Consuming Peroxidases in the Leaf Apoplast of Cowpea in Manganese Tolerance

et al. 2006

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The apoplast is considered the leaf compartment decisive for manganese (Mn) toxicity and tolerance in cowpea (Vigna unguiculata). Particularly apoplastic peroxidases (PODs) were proposed to be key enzymes in Mn toxicity-induced processes. The presented work focuses on the characterization of the role of hydrogen peroxide (H 2 O 2 )-producing (NADH peroxidase) and H 2 O 2 -consuming peroxidase (guaiacol POD) in the apoplastic washing fluid (AWF) of leaves for early stages of Mn toxicity and genotypic differences in Mn tolerance of cowpea. Leaf AWF of the Mn-sensitive cultivar (cv) TVu 91 but not of the Mntolerant cv 1987 showed an increase of guaiacol-POD and NADH-peroxidase activities at elevated AWF Mn concentrations. two-dimensional resolutions of AWF proteins revealed that cv TVu 91 expressed more and additional proteins at high Mn treatment, whereas Mn-tolerant cv TVu 1987 remained nearly unaffected. In both cultivars, NADH-peroxidase activity and accompanied H 2 O 2 formation rate in vitro were significantly affected by Mn 21 , p-coumaric acid, and metabolites occurring in the AWF. The total phenol concentration in the AWF was indicative of advanced stages of Mn toxicity but was rather unrelated to early stages of Mn toxicity and genotypic differences in Mn tolerance. The NADH oxidation by AWF PODs was significantly delayed or enhanced in the presence of the protein-free AWF from cv TVu 1987 or cv TVu 91, respectively. High-performance liquid chromatography analysis of AWF indicates the presence of phenols in cv TVu 1987 not observed in cv TVu 91. We conclude from our studies that the H 2 O 2 -producing NADH peroxidase and its modulation by stimulating or inhibiting phenolic compounds in the leaf apoplast play a major role for Mn toxicity and Mn tolerance in cowpea.

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Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance

Cited by 228 publications

References 51 publications

Characterization of a cDNA from Beta maritima that confers nickel tolerance in yeast

Characterization of a cDNA from Beta maritima that confers nickel tolerance in yeast

A secretory pathway-localized cation diffusion facilitator confers plant manganese tolerance

The Role of Hydrogen Peroxide-Producing and Hydrogen Peroxide-Consuming Peroxidases in the Leaf Apoplast of Cowpea in Manganese Tolerance

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