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Microbiology 148 (2002), 1225-1232
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Microbiology (2002), 148, 1225-1232.
© 2002 Society for General Microbiology


Research Paper

Difference in substrate specificity divides the yeast alkali-metal-cation/H+ antiporters into two subfamilies

Olga Kinclová1,2, Serge Potier2 and Hana Sychrová1

Department of Membrane Transport, Institute of Physiology CzAcadSci, 14220 Prague 4, Czech Republic1
Laboratory of Microbiology and Genetics, UPRES A-7010-CNRS, Université Louis Pasteur, 67083 Strasbourg, France2

Author for correspondence: Hana Sychrová. Tel: +420 2 475 26 67. Fax: +420 2 475 24 88. e-mail: sychrova{at}biomed.cas.cz

Yeast plasma membrane Na+/H+ antiporters (TC 2.A.36) share a high degree of similarity at the protein level. Expression of four antiporters (Saccharomyces cerevisiae Nha1p, Candida albicans Cnh1p, Zygosaccharomyces rouxii ZrSod2-22p and Schizosaccharomyces pombe sod2p) in a Sacch. cerevisiae mutant strain lacking both Na+-ATPase and Na+/H+ antiporter genes made it possible to study the transport properties and contribution to cell salt tolerance of all antiporters under the same conditions. The ZrSod2-22p of the osmotolerant yeast Z. rouxii has the highest transport capacity for lithium and sodium but, like the Schiz. pombe sod2p, it does not recognize K+ and Rb+ as substrates. The Sacch. cerevisiae Nha1p and C. albicans Cnh1p have a broad substrate specificity for at least four alkali metal cations (Na+, Li+, K+, Rb+), but their contribution to overall cell tolerance to high external concentration of toxic Na+ and Li+ cations seems to be lower compared to the antiporters of Schiz. pombe and especially Z. rouxii.

Keywords: Na+ efflux, K+ efflux, salt tolerance, transport




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O. Kinclova-Zimmermannova and H. Sychrova
Plasma-membrane Cnh1 Na+/H+ antiporter regulates potassium homeostasis in Candida albicans
Microbiology, August 1, 2007; 153(8): 2603 - 2612.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
O. Kinclova-Zimmermannova, M. Zavrel, and H. Sychrova
Identification of Conserved Prolyl Residue Important for Transport Activity and the Substrate Specificity Range of Yeast Plasma Membrane Na+/H+ Antiporters
J. Biol. Chem., August 26, 2005; 280(34): 30638 - 30647.
[Abstract] [Full Text] [PDF]




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