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J. Biol. Chem., Vol. 263, Issue 6, 2668-2672, Feb, 1988
LS Tobacman
The length and amino acid sequence of the amino-terminal region of troponin
T (TnT) is regulated by alternative mRNA processing in both mammals and
birds. To study the function of this region, three forms of bovine cardiac
TnT were compared: isoforms TnT1 and TnT2, which differ by the presence or
absence of residues 15-19 and TnT 39-284. TnT 39-284 was prepared by
chemical cleavage of TnT1 at Cys-39. All three forms of TnT successfully
reconstituted with troponin I and troponin C, resulting in troponins
designated Tn1, Tn2, and TnCN. Three properties of the reconstituted
troponins were compared. 1) Tn1 and TnCN had indistinguishable effects on
tropomyosin polymerization. Addition of either 8 microM Tn1 or 8 microM
TnCN increased the viscosity (eta rel) of 5 microM tropomyosin from 1.0 to
1.63 at 10 degrees C. 2) All of the three troponins conferred Ca2+
dependence to the MgATPase rate of myosin S-1-actin-tropomyosin. In the
presence of saturating concentrations of Tn2, Tn1, or TnCN, 50% MgATPase
activation occurred at pCa 6.0, 5.9, or 5.75, respectively. 3) The affinity
of the Ca2+- specific binding site of reconstituted Tn1 was 50% stronger
than the affinity of the same site on TnCN. These results suggest that the
amino- terminal region of cardiac TnT is not a completely Ca2+-insensitive
domain, but rather modulates the interaction of Ca2+ with troponin and with
the thin filament. Furthermore, the effects of TnT on tropomyosin-
tropomyosin binding are predominantly due to portions of TnT carboxyl-
terminal to residue 38.
Structure-function studies of the amino-terminal region of bovine cardiac troponin T
Department of Internal Medicine, University of Iowa, Iowa City 52242.
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