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Amino-acid sequence of the β-subunit of the (Na+ + K+)ATPase deduced from a cDNA

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Abstract

The sodium/potassium-dependent ATPase [(Na+ + K+)ATPase], which establishes and maintains the Na+ and K+ gradients across the plasma membrane of animal cells, consists of two subunits, α and β. Complementary DNA clones encoding the catalytic (α) subunit of sheep kidney1 and Torpedo californica electroplax2 enzymes have previously been isolated and characterized. However, there is little information concerning the primary structure of the β-subunit, a glycoprotein of unknown function and relative molecular mass (Mr) ∼55,000 (ref. 3). Here we describe the isolation and characterization of a cDNA clone containing the entire coding region of the β-subunit of the sheep kidney (Na+ + K+)ATPase. We also discuss structural aspects of the protein and present evidence for a possible evolutionary relationship with the KdpC subunit of the Escherichia coli K+-ATPase4.

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Authors and Affiliations

  1. Departments of Microbiology and Molecular Genetics, University of Cincinnati College of Medicine, 231 Bethesda Avenue, Cincinnati, Ohio, 45267-0524, USA

    Gary E. Shull & Jerry B. Lingrel

  2. Departments of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, 231 Bethesda Avenue, Cincinnati, Ohio, 45267-0524, USA

    Lois K. Lane

Authors
  1. Gary E. Shull
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  2. Lois K. Lane
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  3. Jerry B. Lingrel
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Shull, G., Lane, L. & Lingrel, J. Amino-acid sequence of the β-subunit of the (Na+ + K+)ATPase deduced from a cDNA. Nature 321, 429–431 (1986). https://doi.org/10.1038/321429a0

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