A protein friction model of the actin sliding movement generated by myosin in mixtures of MgATP and MgGTP in vitro.

The sliding movement of an actin filament generated by myosin heads with MgGTP bound is much slower than that by those with MgATP bound. Nonetheless, there is a report that the actin sliding velocity at low (11-21 microM) MgATP concentrations is increased by the addition of MgGTP in a range of 1-3 mM, although the actin sliding velocity at these MgATP concentrations is larger than the maximum sliding velocity attained in the presence of MgGTP alone. The convex rise in the velocity was called "mutual sensitization of MgATP and MgGTP" in the report. Here we propose a theoretical model to account for the mutual sensitization of MgATP and MgGTP. The model is an extension of a protein friction model, accommodating the presence of two different substrates and assuming the presence of motile and non-motile myosins. This new model is in accord with the characteristics of the actin/myosin sliding movement experimentally observed in mixtures of MgATP and MgGTP. Comparison of the model with the experimental results implies that the non-motile and motile myosins are those with the "converse and correct" orientations of their heads with respect to the direction of the actin sliding movement in vitro. Copyright 1999 Academic Press.