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J Biol Chem, Vol. 273, Issue 17, 10594-10601, April 24, 1998

Regulatory Properties of the NH₂- and COOH-terminal Domains of Troponin T
ATPase ACTIVATION AND BINDING TO TROPONIN I AND TROPONIN C

From the Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, CP 26.077, 05599-970 São Paulo SP, Brazil

The contraction of skeletal muscle is regulated by Ca²⁺ binding to troponin C, which results in an internal reorganization of the interactions within the troponin-tropomyosin complex. Troponin T is necessary for Ca²⁺-dependent inhibition and activation of actomyosin. Troponin T consists of an extended NH₂-terminal domain that interacts with tropomyosin and a globular COOH-terminal domain that interacts with tropomyosin, troponin I, and troponin C. In this study we used recombinant troponin T and troponin I fragments to delimit further the structural and regulatory interactions with the thin filament. Our results show the following: (i) the NH₂-terminal region of troponin T activates the actomyosin ATPase in the presence of tropomyosin; (ii) the interaction of the globular domain of troponin T with the thin filament blocks ATPase activation in the absence of Ca²⁺; and (iii) the COOH-terminal region of the globular domain anchors the troponin C-troponin I binary complex to troponin T through a direct Ca²⁺-independent interaction with the NH₂-terminal region of troponin I. This interaction is required for Ca²⁺-dependent activation of the actomyosin ATPase activity. Based on these results we propose a refined model for the troponin complex and its interaction with the thin filament.

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