Role of ATP in the binding of caldesmon to smooth muscle myosin.

We have reported earlier that ATP causes both an increase in the affinity of caldesmon for smooth muscle myosin and a change in stoichiometry from 2 caldesmon molecules per myosin to 1:1 (Hemric & Chalovich, 1990). We now show that this ATP effect does not occur with skeletal muscle myosin, indicating that ATP has a specific effect on the structure of filamentous smooth muscle myosin. This ATP effect does not appear to be due to stabilization of a 10S type of filamentous smooth muscle myosin like that reported earlier (Ikebe & Hartshorne, 1984) since neither phosphorylation nor extensive modification of myosin with MalNEt (both which stabilize the 6S state of monomeric myosin) eliminates the effect of ATP. Caldesmon does bind more tightly to a form of smooth muscle myosin which is resistant to papain digestion. These results suggest that the ATP effect is due to stabilization of a local conformation of smooth muscle myosin which is independent of the larger 10S/6S conformational change (Suzuki et al., 1988). In the presence of ATP, the two heads of smooth muscle muscle myosin and the S-2 region form a single, higher affinity binding region for caldesmon.