PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection

Permanent URI for this collectionhttps://hdl.handle.net/11147/7645

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  • Article
    Citation - WoS: 5
    Citation - Scopus: 4
    Characterization of a Cdna From Beta Maritima That Confers Nickel Tolerance in Yeast
    (Elsevier Ltd., 2014) Bozdağ, Gönensin Ozan; Kaya, Alaattin; Karakaya, Hüseyin Çağlar; Noll, Gundula A.; Prüfer, Dirk; Koç, Ahmet; 04.03. Department of Molecular Biology and Genetics; 04. Faculty of Science; 01. Izmir Institute of Technology
    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.
  • Article
    Citation - WoS: 33
    Citation - Scopus: 40
    Characterization of Two Genes Encoding Metal Tolerance Proteins From Beta Vulgaris Subspecies Maritima That Confers Manganese Tolerance in Yeast
    (Springer Verlag, 2013) Erbaşol, Işıl; Bozdağ, Gönensin Ozan; Koç, Ahmet; Pedas, Pia; Karakaya, Hüseyin Çağlar; Karakaya, Hüseyin Çağlar; 04.03. Department of Molecular Biology and Genetics; 04. Faculty of Science; 01. Izmir Institute of Technology
    Manganese (Mn2+) is an essential micronutrient in plants. However increased Mn2+ levels are toxic to plant cells. Metal tolerance proteins (MTPs), member of cation diffusion facilitator protein (CDF) family, have important roles in metal homeostatis in different plant species and catalyse efflux of excess metal ions. In this study, we identified and characterized two MTP genes from Beta vulgaris spp. maritima (B. v. ssp. maritima). Overexpression of these two genes provided Mn tolerance in yeast cells. Sequence analyses displayed BmMTP10 and BmMTP11as members of the Mn-CDF family. Functional analyses of these proteins indicated that they are specific to Mn2+ with a role in reducing excess cellular Mn2+ levels when expressed in yeast. GFP-fusion constructs of both proteins localized to the Golgi apparatus as a punctuated pattern. Finally, Q-RT-PCR results showed that BmMTP10 expression was induced threefold in response to the excess Mn2+ treatment. On the other hand BmMTP11 expression was not affected in response to excess Mn2+ levels. Thus, our results suggest that the BmMTP10 and BmMTP11 proteins from B. v. ssp. maritima have non-redundant functions in terms of Mn2+ detoxification with a similar in planta localization and function as the Arabidopsis Mn-CDF homolog AtMTP11 and this conservation shows the evolutionary importance of these vesicular proteins in heavy metal homeostatis among plant species.