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Volume 270, Number 13, Issue of March 31, 1995 pp. 7125-7133
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Kinetics of the Interaction of Myosin Subfragment-1 with G-Actin
EFFECT OF NUCLEOTIDES AND DNaseI

(Received for publication, October 19, 1994; and in revised form, December 19, 1994)

Laurent Blanchoin ,  Stéphane Fievez ,  Franck Travers ,  Marie-France Carlier ,  Dominique Pantaloni

The kinetics of interaction of monomeric pyrenyllabeled G-actin with myosin subfragment-1 (S(1) (A(1)) and S(1)(A(2)) isomers) has been examined in the stopped-flow at low ionic strength. The data confirm the previously reported existence of binary GS and ternary G(2)S complexes. The increase in pyrenyl-actin fluorescence which monitors the G-actin-S1 interactions is linked to the isomerization of these complexes following rapid equilibrium binding steps. The rates of isomerization are 200 s for GS and 50 s for G(2)S at 4 °C and in the absence of ATP. DNaseI and S(1) bind G-actin essentially in a mutually exclusive fashion. Both GS and G(2)S are dissociated by MgATP and MgADP. The kinetics and mechanism of ATP-induced dissociation of G(2)S are quantitatively close to the ATP-induced dissociation of F-actin-S(1), which indicates the G(2)S is a good model for the F-actin-S(1) interface. GS and G(2)S display different kinetic behaviors in response to nucleotides, GS being less efficiently dissociated than G(2)S by MgATP. This result suggests that different mechanical properties of the cross-bridge might correlate with different orientations of the myosin head and different actin/myosin binding ratios.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.