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Originally published In Press as doi:10.1074/jbc.M211016200 on December 2, 2002

J. Biol. Chem., Vol. 278, Issue 7, 4410-4415, February 14, 2003
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Both Heads of Tissue-derived Smooth Muscle Heavy Meromyosin Bind to Actin in the Presence of ADP*

Patricia A. Ellison, Zachary S. DePew, and Christine R. CremoDagger

From the Department of Biochemistry, University of Nevada, Reno, Nevada 89557

The effect of ADP and phosphorylation upon the actin binding properties of heavy meromyosin was investigated using three fluorescence methods that monitor the number of heavy meromyosin heads that bind to pyrene-actin: (i) amplitudes of ATP-induced dissociation, (ii) amplitudes of ADP-induced dissociation of the pyrene-actin-heavy meromyosin complex, and (iii) amplitudes of the association of heavy meromyosin with pyrene-actin. Both heads bound to pyrene-actin, irrespective of regulatory light chain phosphorylation or the presence of ADP. This behavior was found for native regulated heavy meromyosin prepared by proteolytic digestion of chicken gizzard myosin with between 5 and 95% heavy chain cleavage at the actin-binding loop, showing that two-head binding is a property of heavy meromyosin with uncleaved heavy chains. These data are in contrast to a previous study using an uncleaved expressed preparation (Berger, C. E., Fagnant, P. M., Heizmann, S., Trybus, K. M., and Geeves, M. A. (2001) J. Biol. Chem. 276, 23240-23245), which showed that one head of the unphosphorylated heavy meromyosin-ADP complex bound to actin and that the partner head either did not bind or bound weakly. Possible explanations for the differences between the two studies are discussed. We have shown that unphosphorylated heavy meromyosin appears to adopt a special state in the presence of ADP based upon analysis of actin-heavy meromyosin association rate constants. Data were consistent with one head binding rapidly and the second head binding more slowly in the presence of ADP. Both heads bound to actin at the same rate for all other states.

* This work was supported by National Institutes of Health Grant AR40917. Research supported in part by Nevada Agricultural Research Station publication number 0302355.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.

Dagger Corresponding author: Dept. of Biochemistry/330, 1664 N. Virginia St., University of Nevada, Reno, Reno, Nevada 89557. Tel.: 775-784-7033; Fax: 775-784-1419; E-mail: cremo@unr.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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