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J. Biol. Chem., Vol. 263, Issue 21, 10082-10087, 07, 1988
JP Vaillancourt, C Lyons and GP Cote
We have previously purified and characterized a Dictyostelium myosin II
heavy chain kinase which phosphorylates threonine residues (Cote, G. P.,
and Bukiejko, U. (1987) J. Biol. Chem. 262, 1065-1072). The phosphorylated
threonines are located within a 34-kDa fragment which can be selectively
cleaved from the carboxyl terminal end of the Dictyostelium myosin II tail.
Tryptic and chymotryptic digests of the 34-kDa fragment phosphorylated with
the kinase have now been performed and the resulting phosphopeptides
isolated and sequenced. Two phosphorylated threonine residues have been
identified, corresponding to residues 1833 and 2029 in the complete amino
acid sequence of the Dictyostelium myosin II heavy chain. These amino acids
are 87 and 283 residues, respectively, distant from the carboxyl terminus
of the Dictyostelium myosin II heavy chain and are present in sections of
the tail which seem to be alpha-helical coiled coils. In contrast, the
three Acanthamoeba myosin II heavy chain phosphorylation sites are located
within 10 residues of each other in a small globular domain at the carboxyl
terminal tip of the tail (Cote, G. P., Robinson, E. A., Appella, E., and
Korn, E. D. (1984) J. Biol. Chem. 259, 12781-12787). This suggests that the
mechanism by which heavy chain phosphorylation inhibits the actin-activated
ATPase activity and filament-forming properties of the two myosins may be
quite different.
Identification of two phosphorylated threonines in the tail region of Dictyostelium myosin II
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.
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