one of the two antiporters, Spsod2 was the very fi


one of the two antiporters, Spsod2 was the very first characterized yeast transport system with an Na+/H+ antiport mechanism (Jia et al., 1992). Its identification was based on a selection for increased tolerance to Li+ in salt-sensitive S. pombe cells. Deletion of the gene led to diminished NaCl tolerance, its overexpression resulted in an increased Na+ export from cells and the heterologous expression in S. cerevisiae cells confirmed the antiporter’s role in sodium efflux and tolerance, as well as its inability to transport potassium cations (Jia et al., 1992). Much Ixazomib datasheet later, the second S. pombe antiporter (SpSod22) was identified, and its characterization, though only via expression in S. cerevisiae, showed that it efficiently transports K+ and is thus probably the main system for the maintenance of potassium homeostasis in S. pombe cells exposed to surplus

K+ cations (Papouskova & Sychrova, 2007). The Y. lipolytica genome also contains two genes encoding members of the NHA family (Papouskova & Sychrova, 2006). Their heterologous expression in S. cerevisiae cells revealed that while the YlNha1 protein mainly increased cell tolerance to potassium and contributed to potassium homeostasis in the presence of very high concentrations of extracellular KCl, YlNha2p displayed a remarkable transport capacity for sodium, in fact, the highest so far measured for any yeast Na+/H+ antiporter. The two plasma-membrane antiporters of the osmotolerant yeast Z. rouxii (ZrSod2-22 and ZrNha1) have been selleck chemicals llc characterized in detail both in S. cerevisiae and in Z. rouxii cells. First, Bumetanide the sodium-specific Sod2 (and its silent copy Sod22) from

a highly salt-tolerant strain (ATCC 4298) and later the Sod2-22 from the less halotolerant CBS732 strain were characterized upon expression in S. cerevisiae (Iwaki et al., 1998; Kinclova et al., 2001b). Both ZrSod2 and ZrSod22 were shown to enhance the NaCl tolerance of a salt-sensitive S. cerevisiae strain, but only ZrSOD2 was confirmed to be transcribed in Z. rouxii cells (Watanabe et al., 1995; Iwaki et al., 1998), so the high salt tolerance of the Z. rouxii ATCC 4298 strain was not based on the presence and expression of two copies of genes encoding a sodium-specific Na+/H+ antiporter. Only one copy of the SOD2 gene has been found in the Z. rouxii CBS732 genome. As it was not only highly identical to ZrSOD2 but also contained a sequence unique to ZrSOD22, it was named ZrSOD2-22 (Kinclova et al., 2001b). Heterologous expression in an S. cerevisiae strain lacking its own alkali–metal–cation exporters revealed that all three Z. rouxii SOD antiporters transport only sodium and lithium (Iwaki et al., 1998; Kinclova et al., 2001b, 2002), similar to the S. pombe sod2 antiporter. A later search for a putative potassium–proton antiporter in Z. rouxii led to the identification of the ZrNHA1 gene, and characterization of its product in S.

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