The decrease in flexibility of actin filaments induced by tropomyosin or Ca-unsaturated troponin-tropomyosin complex increases the cooperativity of conformational changes of actin induced by myosin subfragment-1.
Does not inform clinical decisions; leaves open how actin cooperativity modulates cardiac thin-filament regulation in vivo.
The interaction of regulated and unregulated actin of myosin-free ghost single fibre with myosin subfragment-1 free of 5,5'-dithiobis(2-nitrobenzoic acid) light chains was investigated by polarized microphotometry. The anisotropy of intrinsic tryptophan fluorescence of regulated actin is Ca2+-dependent and has a maximal value at low (pCa greater than or equal to 7) and a minimal value at high (pCa less than or equal to 6) concentrations of Ca2+. The interaction of myosin subfragment-1 with actin induces cooperative changes in actin structure, which manifest themselves in a decrease in the anisotropy of tryptophan fluorescence. The cooperativity of conformational changes in actin, induced by myosin subfragment-1, is high for regulated actin in the absence of Ca2+ and low for unregulated and regulated actin in the presence of Ca2+. The data obtained suggest that the decrease of the flexibility of actin filaments, induced by tropomyosin or by Ca-unsaturated troponin-tropomyosin complex, results in increased cooperativity of conformational changes of actin induced by myosin subfragment-1.
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Borovikov et al. (1983) studied this question.
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