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Originally published In Press as doi:10.1074/jbc.M206115200 on July 10, 2002

J. Biol. Chem., Vol. 277, Issue 38, 35202-35209, September 20, 2002
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New Insights into the Role of the N Terminus in Conformational Transitions of the Na,K-ATPase*

Laura SegallDagger , Lois K. Lane§, and Rhoda BlosteinDagger

From the Dagger  Department of Biochemistry, McGill University, Quebec H3G 1A4, Canada and the § Department of Pharmacology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0575

The deletion of 32 residues from the N terminus of the alpha 1 catalytic subunit of the rat Na,K-ATPase (mutant alpha 1M32) shifts the E1/E2 conformational equilibrium toward E1, and the combination of this deletion with mutation E233K in the M2-M3 loop acts synergistically to shift the conformation further toward E1 (Boxenbaum, N., Daly, S. E., Javaid, Z. Z., Lane, L. K., and Blostein, R. (1998) J. Biol. Chem. 273, 23086-23092). To delimit the region of the cytoplasmic N terminus involved in these interactions, the consequences of a series of N-terminal deletions of alpha 1 beyond Delta 32 were evaluated. Criteria to assess shifts in conformational equilibrium were based on effects of perturbation of the entire catalytic cycle ((i) sensitivity to vanadate inhibition, (ii) K+ sensitivity of Na-ATPase measured at micromolar ATP, (iii) changes in K'ATP, and (iv) catalytic turnover), as well as estimates of the rates of the conformational transitions of phospho- and dephosphoenzyme (E1P right-arrow E2P and E2(K+) right-arrow E1 + K+). The results show that, compared with alpha 1M32, the deletion of up to 40 residues (alpha 1M40) further shifts the poise toward E1. Remarkably, further deletions (mutants alpha 1M46, alpha 1M49, and alpha 1M56) reverse the effect, such that these mutants increasingly resemble the wild type alpha 1. These results suggest novel intramolecular interactions involving domains within the N terminus that impact the manner in which the N terminus/M2-M3 loop regulatory domain interacts with the M4-M5 catalytic loop to effect E1 left-right-arrow E2 transitions.

* This work was supported by operating grants from the Canadian Institutes of Health Research (Grant MT-3876) and the Quebec Heart and Stroke Foundation (to R. B.), the National Institutes of Health (Grant HL 49204) (to L. K.), and a predoctoral fellowship from the Heart and Stroke Foundation of Canada (to L. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Montreal General Hospital Research Inst., 1650 Cedar Ave., Rm. L11-132, Montreal, Quebec H3G 1A4, Canada. Tel.: 514-934-1934 (ext. 44501); Fax: 514-934-8332; E-mail: Rhoda.Blostein@mcgill.ca.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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