Structural analysis of the products of chymotryptic cleavage of the E1 form of Na,K-ATPase alpha-subunit: identification of the N-terminal fragments containing the transmembrane H1-H2 domain

FEBS Letters
A IvanovN N Modyanov

Abstract

Chymotryptic cleavage of the Na,K-ATPase in NaCl medium abolishes ATPase activity and alters other functional parameters. The structure of this modified enzyme is uncertain since only one product of selective proteolysis, the 83-kDa fragment of the alpha-subunit (Ala267-C-terminus) has been identified previously. Here, we applied additional tryptic digestion followed by oxidative cross-linking to identify the products originating from the N-terminal part of the alpha-subunit. These fragments start at Ala72 or Thr74 and contain the transmembrane H1-H2 domain. Formation of cross-linked product between alpha-fragments containing H1-H2 and H7-H10 demonstrate that the structural integrity of the membrane moiety is preserved. We also determined that secondary cleavage of the 83-kDa fragment leads to the formation of C-terminal 48-kDa alpha-fragments with multiple N-termini at Ile582, Ser583, Met584 and Ile585.

References

Jun 8, 1987·FEBS Letters· Ovchinnikov YuAK N Dzhandzugazyan KN=Dzhadzhugazyan
Aug 15, 1995·Proceedings of the National Academy of Sciences of the United States of America·S LutsenkoJ H Kaplan
Jun 30, 1995·The Journal of Biological Chemistry·M GanjeizadehA Askari
May 6, 1996·Biochimica Et Biophysica Acta·J V MøllerM le Maire
Mar 21, 1997·The Journal of Biological Chemistry·N A SarvazyanA Askari

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