J. Biol. Chem., Vol. 262, Issue 24, 11410-11412, 08, 1987
F-actin-binding synthetic heptapeptide having the amino acid sequence around the SH1 cysteinyl residue of myosin
R Suzuki, N Nishi, S Tokura and F Morita
The heptapeptide Ile-Arg-Ile-Cys-Arg-Lys-Gly-ethyl ester, having the amino
acid sequence around the SH1 of myosin heavy chain, was coprecipitated with
F-actin after ultracentrifugation. The heptapeptide inhibited the formation
of acto-S-1 rigor complex by competing with S-1 for actin. Assuming a
simple competitive inhibition, the dissociation constant of
acto-heptapeptide complex was evaluated as 0.23 mM. An N- terminal
tripeptide derivative from the heptapeptide Ile-Arg-Ile-methyl ester also
formed a complex with F-actin with a dissociation constant of 1.1 mM.
However, the other piece, Cys-Arg-Lys-Gly-ethyl ester, and a tetrapeptide,
Val-Leu-Glu-Gly-ethyl ester, having the sequence adjacent to the N-terminal
of the heptapeptide, scarcely bound with F-actin. These results suggest
that part of the actin-binding site of myosin heavy chain around SH1
(Katoh, T., Katoh, H., and Morita, F. (1985) J. Biol. Chem. 260, 6723-6727)
has the sequence of Ile-Arg-Ile and it is located adjacent to SH1 on its
N-terminal side.