Role of highly conserved lysine 130 of myosin motor domain. In vivo and in vitro characterization of site specifically mutated myosin.
KM Ruppel, TQ Uyeda, JA Spudich - Journal of Biological Chemistry, 1994 - ASBMB
We have created a mutant Dictyostelium myosin II heavy chain gene in which a highly
conserved lysine residue (Lys-130) is changed to leucine. Lys-130 is a residue that is known
to be trimethylated in skeletal muscle myosin and had been thought to play an integral role
in the interaction of myosin with ATP during the actomyosin chemomechanical cycle. We
report here the first in vivo and in vitro characterization of an engineered missense mutation
in the motor domain of myosin. Expression of the K130L myosin in a Dictyostelium strain that …
conserved lysine residue (Lys-130) is changed to leucine. Lys-130 is a residue that is known
to be trimethylated in skeletal muscle myosin and had been thought to play an integral role
in the interaction of myosin with ATP during the actomyosin chemomechanical cycle. We
report here the first in vivo and in vitro characterization of an engineered missense mutation
in the motor domain of myosin. Expression of the K130L myosin in a Dictyostelium strain that …