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J Biol Chem, Vol. 274, Issue 24, 16681-16684, June 11, 1999

COMMUNICATION
Effects of Troponin I Phosphorylation on Conformational Exchange in the Regulatory Domain of Cardiac Troponin C

Vadim Gaponenko, Ekram Abusamhadneh, M. Bret Abbott, Natosha Finley, Genevieve Gasmi-Seabrook, R. John Solaro, Mark Rance, and Paul R. Rosevear

From the Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, College of Medicine, Cincinnati, Ohio 45267 and the  Department of Physiology and Biophysics, College of Medicine, University of Illinois, Chicago, Illinois 60612

Conformational exchange has been demonstrated within the regulatory domain of calcium-saturated cardiac troponin C when bound to the NH₂-terminal domain of cardiac troponin I-(1-80), and cardiac troponin I-(1-80)DD, having serine residues 23 and 24 mutated to aspartate to mimic the phosphorylated form of the protein. Binding of cardiac troponin I-(1-80) decreases conformational exchange for residues 29, 32, and 34. Comparison of average transverse cross correlation rates show that both the NH₂- and COOH-terminal domains of cardiac troponin C tumble with similar correlation times when bound to cardiac troponin I-(1-80). In contrast, the NH₂- and COOH-terminal domains in free cardiac troponin C and cardiac troponin C bound cardiac troponin I-(1-80)DD tumble independently. These results suggest that the nonphosphorylated cardiac specific NH₂ terminus of cardiac troponin I interacts with the NH₂-terminal domain of cardiac troponin C.

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