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Volume 270, Number 26, Issue of June 30, pp. 15707-15710, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Interactions of Phosphorylation and Dimerizing Domains of the -Subunits of Na/K-ATPase

Mehdi Ganjeizadeh , Nina Zolotarjova , Wu-Hsiung Huang , Amir Askari

Chemical cross-linking studies are among a number of experimental approaches that have suggested the functional significance of higher association states of ,-protomers of Na/K-ATPase. Formation of the phosphointermediate of the enzyme on Asp of the -subunit is known to induce oxidative cross-linking of the -subunits catalyzed by Cu-phenanthroline. To localize the phosphorylation-induced ,-interface, we cleaved at Arg-Ala by controlled proteolysis and exposed the partially cleaved enzyme to the cross-linking reagent. In addition to the ,-dimer, two other phosphorylation-induced cross-linked products were obtained. Using gel electrophoretic resolution of the cross-linked P-labeled enzyme, N-terminal analyses of the products, and their reactivities with sequence-specific antibodies, the two products were identified as a homodimer of the C-terminal 64-kDa fragment of and a heterodimer of and the 64-kDa peptide. The latter dimer was also obtained when the cross-linked ,-dimer was formed first and then subjected to proteolysis. The findings localize the dimerizing domain to the C-terminal side of Ala and indicate that intersubunit proximities of dimerizing domains are regulated by phosphorylation-dephosphorylation of Asp during the reaction cycle of the enzyme.

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