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  • Title: Troponin in both smooth and striated muscles of Ascidian Ciona intestinalis functions as a Ca2+-dependent accelerator of actin−myosin interaction.
    Author: Ohshiro K, Obinata T, Dennisson JG, Ogasawara M, Sato N.
    Journal: Biochemistry; 2010 Nov 09; 49(44):9563-71. PubMed ID: 20849123.
    Abstract:
    Troponin, a Ca2+-dependent regulator of muscle contraction, acts as an inhibitor of the actin−myosin interaction in the absence of Ca2+ during contraction in vertebrate striated muscle. However, variation has been observed in the mode of troponin-dependent regulation among the animals belonging to Protochordata, the taxon most closely related to Vertebrata. Although troponin in striated muscle of a cephalochordate amphioxus functions as an inhibitor in the absence of Ca2+ as in vertebrates [Dennisson, J. G., et al. (2010) Zool. Sci. 27, 461−469], troponin in the smooth muscle of a urochordate ascidian (Halocynthia roretzi) regulates actin−myosin interaction as an activator in the presence of Ca2+ and not an inhibitor in the absence of Ca2+ as in vertebrates [Endo, T., and Obinata, T. (1981) J. Biochem. 89, 1599−1608]. In this study, to further clarify the functional diversity of troponin, we examined the role of troponin in Ca2+-dependent regulation of the actin−myosin interaction in striated and smooth muscles in another member of Ascidiacea (Ciona inetestinalis) using three recombinant troponin components, TnT, TnI, and TnC, produced using an Escherichia coli expression system. On the basis of actomyosin ATPase assays, we show here that troponins in both smooth and striated muscles of ascidian function as a Ca2+-dependent activator of the actin−myosin interaction and TnT is the component responsible for this activation. These results indicate that troponin of ascidian has evolved in a manner different from that of amphioxus and vertebrates in terms of function.
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