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J Biol Chem, Vol. 274, Issue 11, 7157-7164, March 12, 1999

Roles for the Troponin Tail Domain in Thin Filament Assembly and Regulation
A DELETIONAL STUDY OF CARDIAC TROPONIN T

Ashley Hinkle, Angela Goranson, Carol A. Butters, and Larry S. Tobacman^§

From the Departments of  Internal Medicine and ^§ Biochemistry, University of Iowa, Iowa City, Iowa 52242

Striated muscle contraction is regulated by Ca²⁺ binding to troponin, which has a globular domain and an elongated tail attributable to the NH₂-terminal portion of the bovine cardiac troponin T (TnT) subunit. Truncation of the bovine cardiac troponin tail was investigated using recombinant TnT fragments and subunits TnI and TnC. Progressive truncation of the troponin tail caused progressively weaker binding of troponin-tropomyosin to actin and of troponin to actin-tropomyosin. A sharp drop-off in affinity occurred with NH₂-terminal deletion of 119 rather than 94 residues. Deletion of 94 residues had no effect on Ca²⁺-activation of the myosin subfragment 1-thin filament MgATPase rate and did not eliminate cooperative effects of Ca²⁺ binding. Troponin tail peptide TnT1-153 strongly promoted tropomyosin binding to actin in the absence of TnI or TnC. The results show that the anchoring function of the troponin tail involves interactions with actin as well as with tropomyosin and has comparable importance in the presence or absence of Ca²⁺. Residues 95-153 are particularly important for anchoring, and residues 95-119 are crucial for function or local folding. Because striated muscle regulation involves switching among the conformational states of the thin filament, regulatory significance for the troponin tail may arise from its prominent contribution to the protein-protein interactions within these conformations.

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