TY - JOUR
T1 - A functional recombinant myosin II lacking a regulatory light chain-binding site
AU - Uyeda, Taro Q.P.
AU - Spudich, James A.
N1 - Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1993
Y1 - 1993
N2 - 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 to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.
AB - 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 to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.
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U2 - 10.1126/science.8266074
DO - 10.1126/science.8266074
M3 - Article
C2 - 8266074
AN - SCOPUS:0027767689
VL - 262
SP - 1867
EP - 1870
JO - Science
JF - Science
SN - 0036-8075
IS - 5141
ER -