Premium
Role of the C‐terminal extremities of the smooth muscle myosin heavychains" implication for assembly properties
Author(s) -
Sophie QuevillonChéruel,
G. Foucault,
Michel Desmadril,
AnneMarie Lompré,
JeanJacques Béchet
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00827-3
Subject(s) - myosin , circular dichroism , contractility , gene isoform , biophysics , differential scanning calorimetry , chemistry , escherichia coli , recombinant dna , heavy meromyosin , meromyosin , terminal (telecommunication) , crystallography , biochemistry , myosin light chain kinase , myosin head , biology , endocrinology , telecommunications , physics , gene , computer science , thermodynamics
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.