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Journal Article

The Na+,K+-ATPase carrying the carboxy-terminal Ca2+/calmodulin binding domain of the Ca2+ pump has 2Na+,2K+ stoichiometry and lost charge movement in Na+/Na+ exchange

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Yoshimura,  Shige H.
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Faculty of Integrated Human Studies, Kyoto University, Kyoto 606-01, Japan;

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Vasilets,  Larisa A.
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Chemical Physics, Russian Academy of Sciences, 142432 Chernogolovka, Russia;

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Schwarz,  Wolfgang
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Yoshimura, S. H., Vasilets, L. A., Ishii, T., Takeyasu, K., & Schwarz, W. (1998). The Na+,K+-ATPase carrying the carboxy-terminal Ca2+/calmodulin binding domain of the Ca2+ pump has 2Na+,2K+ stoichiometry and lost charge movement in Na+/Na+ exchange. FEBS Letters, 425(1), 71-74. doi:10.1016/s0014-5793(98)00202-6.


Cite as: https://hdl.handle.net/21.11116/0000-0008-392A-A
Abstract
An altered ion-transport stoichiometry from 3Na+,2K+ to 2Na+,2K+ is observed in a chimeric Na+,K+ATPase, which carries the Ca2+/calmodulin binding domain (CBD) of the plasma membrane Ca2+-ATPase at its carboxy-terminus [Zhao et al., FEBS Lett. 408 (1997) 271-2751. The ouabain-resistant mutant of this chimera (ORalpha1-CBD) was constructed to further investigate the effect of the CBD on ion-transport properties. The ORalpha1-CBD still shows the 2Na+,2K+ stoichiometry. The loss of electrogenicity is accompanied by the disappearance of transient charge movements in the Na+/Na+ exchange mode. We conclude that the binding of the third Na+ ion, but not of the two others, in 3Na+,2K+ transport mode apparently senses the electric field, and that the voltage-dependent Na+ binding is likely to be lost in the chimera with CBD.