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  • Title: Subunit function in cardiac myosin. Effects of binding phosphorylated and unphosphorylated myosin light chain 2 to light chain 2-deficient myosin.
    Author: Bhan A, Malhotra A, Scheuer J, Conti MA, Adelstein RS.
    Journal: J Biol Chem; 1981 Aug 10; 256(15):7741-3. PubMed ID: 7263624.
    Abstract:
    The 20,000-dalton light chain of cardiac muscle myosin can be specifically digested and thereby removed from the rest of the myosin molecule by incubation with a myofibrillar protease (Malhotra, A., Huang, S., and Bhan, A. (1979) Biochemistry 18, 461-467). In order to study the effects of phosphorylation of the 20,000-dalton myosin light chain, experiments were carried out with cardiac muscle myosin that was made deficient in this light chain following proteolysis. Both the phosphorylated and unphosphorylated isolated 20,000-dalton myosin light chain of cardiac muscle myosin were found to bind to light chain-deficient myosin. Prior to readdition of the isolated light chains, this light chain-deficient myosin was found to have a higher MgATPase activity in the presence and absence of actin, than native myosin. Binding of the unphosphorylated myosin light chain restored the MgATPase activity of light chain-deficient myosin to that of native cardiac myosin. In contrast, the binding of 2 mol of the previously phosphorylated myosin light chain did not lower the actin-activated MgATPase activity. The results suggest that while phosphorylation of the 20,000-dalton light chain of cardiac muscle myosin is not essential for the actin-activated MgATPase activity, it may have a modulatory role.
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