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We have investigated the effect of the E41K, R91G, and E139del β-tropomyosin (TM) mutations that cause congenital myopathy on the position of TM and orientation of actin monomers and myosin heads at different mimicked stages of the ATPase cycle in troponin-free ghost muscle fibers by polarized fluorimetry. A multi-step shifting of wild-type TM to the filament center accompanied by an increase in the amount of switched on actin monomers and the strongly bound myosin heads was observed during the ATPase cycle. The R91G mutation shifts TM further towards the inner and outer domains of actin at the strong- and weak-binding stages, respectively. The E139del mutation retains TM near the inner domains, while the E41K mutation captures it near the outer domains. The E41K and R91G mutations can induce the strong binding of myosin heads to actin, when TM is located near the outer domains. The E139del mutation inhibits the amount of strongly bound myosin heads throughout the ATPase cycle.

Original publication

DOI

10.1016/j.abb.2015.05.002

Type

Journal article

Journal

Arch Biochem Biophys

Publication Date

07/2015

Volume

577-578

Pages

11 - 23

Keywords

Congenital myopathies, F-actin, Fluorescence polarization, Ghost muscle fibers, Myosin, Tropomyosin, Troponin, Actins, Adenosine Triphosphatases, Animals, Humans, Muscle, Skeletal, Muscular Diseases, Mutation, Myosins, Protein Conformation, Rabbits, Tropomyosin