Invertebrate troponin C typically contains Ca²⁺-specific binding sites, sites II and IV, in the N- and C-terminal domains, respectively. To investigate the roles of these sites for Ca²⁺-dependent regulation of muscle contraction, we generated lobster troponin C mutants, and analyzed their Ca²⁺-binding properties and regulatory effects on actomyosin-tropomyosin Mg-ATPase activity. The results suggest that Ca²⁺ binding to site IV is responsible for regulation at relatively low Ca²⁺ concentrations, while site II has an essential role in full activation at higher Ca²⁺ concentrations.
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