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- W2912673468 abstract "Mutations in the gene TPM1 cause both hypertrophic and dilated cardiomyopathy. Deleterious polymorphisms are found throughout α-tropomyosin, and those within the end-to-end bond regions are poised to drastically change the ability of tropomyosin to bind to actin, affecting the balance of the blocked-closed-open paradigm of muscle contraction regulation. The M8R mutation is found in both α and γ tropomyosins, causing dilated cardiomyopathy and nemaline myopathy respectively. Previous work on pseudo-acetylated and non-acetylated M8R in α-tropomyosin has shown that the mutation causes drastically reduced actin-binding, increased velocity of actin-tropomyosin filaments on myosin, and reduced myosin S1 ATPase. Here we determined the effects of the M8R mutation on the calcium dependence of troponin/tropomyosin regulated in vitro motility of F-actin, its actin-binding at steady state via co-sedimentation, and its structural stability using circular dichroism. The calcium sensitivity of cardiac thin filaments regulated with M8R was increased compared to WT, as was the cooperativity with no change in maximum actin filament velocity. The denaturation of α-tropomyosin followed a sigmoidal relationship, showing that M8R unfolded more gradually when exposed to increasing urea than did WT, but was more sensitive to the presence of urea. Finally, M8R α-tropomyosin binding of F-actin was, as previously reported, extremely low in the absence of S1. The altered regulatory and biochemical properties are consistent with decreased end-end bond stiffness. Using molecular dynamics simulations, mutation-induced alterations in tropomyosin structure around the end-to-end bond are being characterized. Support by HL123774 to JRM." @default.
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- W2912673468 date "2019-02-01" @default.
- W2912673468 modified "2023-09-28" @default.
- W2912673468 title "Functional Implications of Dcm End-to-End Bond Mutation in A-Tropomyosin" @default.
- W2912673468 doi "https://doi.org/10.1016/j.bpj.2018.11.989" @default.
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