The highly conserved extracellular peptide, DSYG(893-896), is a critical structure for sodium pump function

European Journal of Biochemistry
Susanne BeckerGeorgios Scheiner-Bobis

Abstract

The peptide sequence DSYG(893-896) of the sheep sodium pump alpha 1 subunit is highly conserved among all K(+)-transporting P-type ATPases. To obtain information about its function, single mutations were introduced and the mutants were expressed in yeast and analysed for enzymatic activity, ion recognition, and alpha/beta subunit interactions. Mutants of Ser894 or Tyr895 were all active. Conservative phenylalanine and tryptophan mutants of Tyr895 displayed properties that were similar to the properties of the wild-type enzyme. Replacement of the same amino acid by cysteine, however, produced heat-sensitive enzymes, indicating that the aromatic group contributes to the stability of the enzyme. Mutants of the neighbouring Ser894 recognized K(+) with altered apparent affinities. Thus, the Ser894-->Asp mutant displayed a threefold higher apparent affinity for K(+) (EC(50) = 1.4 +/- 0.06 mm) than the wild-type enzyme (EC(50) = 3.8 +/- 0.33 mm). In contrast, the mutant Ser894-->Ile had an almost sixfold lower apparent affinity for K(+) (EC(50) = 21.95 +/- 1.41 mm). Mutation of Asp893 or Gly896 produced inactive proteins. When an anti-beta 1 subunit immunoglobulin was used to co-immunoprecipitate the alpha 1 subunit, neither the Gly89...Continue Reading

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May 25, 2002·European Journal of Biochemistry·Georgios Scheiner-Bobis

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Citations

Nov 26, 2010·Cardiovascular Research·Georgios Scheiner-Bobis
Nov 30, 2019·Parasite : Journal De La Société Française De Parasitologie·John C Meade
Jul 4, 2007·Human Molecular Genetics·Svetlana GorokhovaNathaniel Heintz
Apr 28, 2021·Journal of Chemical Theory and Computation·Alexander van Teijlingen, Tell Tuttle
Aug 5, 2008·Archives of Biochemistry and Biophysics·Ramón CocaFrancisco Fernández-Belda

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