Self-association of plasma membrane Ca(2+)-ATPase by volume exclusion

FEBS Letters
D Kosk-KosickaV L Lew

Abstract

At enzyme concentrations above 40 nM the configuration of the purified plasma membrane Ca(2+)-ATPase is that of calmodulin-insensitive dimers. Dilution of the enzyme generates progressively higher proportions of calmodulin-sensitive monomers with lower Vmax and Ca2+ sensitivity than the dimeric enzyme. Dimerization from monomeric state had not been documented before. We investigated whether concentration by volume exclusion, obtained by addition of a large molecular weight dextran to a monomeric Ca(2+)-ATPase would elicit dimer-like behavior. Dextran induced self-association of monomers, as monitored by fluorescence energy transfer, but the Ca2+ sensitivity of the re-associated monomers was lower than that of the native dimers. These results suggest that the self-association reaction is structurally but not functionally reversible, and also document the existence of a hitherto unknown kinetic state of the oligomerized Ca(2+)-ATPase, with high Vmax but low Ca(2+)-sensitivity.

References

Sep 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·B GrasbergerH Metzger
Aug 25, 1971·European Journal of Biochemistry·T C Laurent
Nov 15, 1983·Biochemical and Biophysical Research Communications·A M MinocherhomjeeB D Roufogalis
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Jan 1, 1993·Annual Review of Biophysics and Biomolecular Structure·S B Zimmerman, A P Minton

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Citations

Sep 4, 2004·Biophysical Journal·Brian M Baynes, Bernhardt L Trout
Dec 26, 2001·Biophysical Journal·Valeria LeviF Luis González Flecha
Apr 26, 1996·The Journal of Biological Chemistry·D L Sackett, D Kosk-Kosicka

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