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Updated: Jul 21, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Role of the C-terminal extremities of the smooth muscle myosin heavy chains: implication for assembly properties
S Quevillon-Chéruel1, G Foucault, M Desmadril
1Laboratoire des Gènes et Protéines Musculaires, CNRS EP 1088, Université de Paris-Sud, Orsay, France.
Abstract:
The two light meromyosin isoforms from rabbit smooth muscle were prepared as recombinant proteins in Escherichia coli. These species which differed only by their C-terminal extremity showed the same circular dichroism spectra and endotherms in measurements of differential scanning calorimetry. Their solubility properties were different at pH 7.0 in the absence of monovalent salts. Their paracrystals formed at low pH differed by their aspect and number. These data suggest a role for the C-terminal extremity of myosin heavy chains in the assembly of myosin molecules in filaments and consequently in the contractility of smooth muscles.
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