A functional recombinant myosin II lacking a regulatory light chain-binding site.

@article{Uyeda1993AFR,
  title={A functional recombinant myosin II lacking a regulatory light chain-binding site.},
  author={Taro Q. P. Uyeda and James A Spudich},
  journal={Science},
  year={1993},
  volume={262 5141},
  pages={1867-70}
}
Myosin II, which converts the energy of adenosine triphosphate hydrolysis into the movement of actin filaments, is a hexamer of two heavy chains, two essential light chains, and two regulatory light chains (RLCs). Dictyostelium myosin II is known to be regulated in vitro by phosphorylation of the RLC. Cells in which the wild-type myosin II heavy chain was replaced with a recombinant form that lacks the binding site for RLC carried out cytokinesis and almost normal development, processes known… CONTINUE READING
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