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J. Biol. Chem., Vol. 265, Issue 27, 16138-16144, 09, 1990
H Brzeska, TJ Lynch, B Martin, A Corigliano-Murphy and ED Korn
Phosphorylation of a single threonine (myosin IA) or serine (myosins IB and
IC) in the heavy chains of the Acanthamoeba myosin I isozymes is required
for expression of their actin-activated Mg2(+)-ATPase activities. We now
report that the synthetic peptide Gly-Arg-Gly-Arg- Ser-Ser-Val-Tyr-Ser,
which corresponds to the phosphorylated region of Acanthamoeba myosin IC,
is a good substrate for myosin I heavy chain kinase: Km = 54 microM, and
Vmax = 15 mumols/min.mg. The same serine is phosphorylated as in the native
substrate (residue 6 in the above sequence), and kinase activity with the
synthetic peptide as substrate is also stimulated by
phosphatidylserine-enhanced autophosphorylation of the kinase. These
results indicate that all of the essential sequence determinants of kinase
specificity are contained within this 9- residue peptide. With the peptide
as substrate, we found that another acidic phospholipid,
phosphatidylinositol, also enhances autophosphorylation of the kinase
whereas the neutral phospholipids phosphatidylcholine and
phosphatidylethanolamine do not. By comparing the Km and Vmax values for a
series of synthetic peptide substrates, we established that 1 basic amino
acid is essential on the NH2-terminal side of the phosphorylation site, and
two are preferable, and that a tyrosine is essential 2 residues away on the
COOH-terminal side. There is a slight preference for arginines over
lysines. All of these local sequence specificity determinants are present
in the three native substrates, Acanthamoeba myosins IA, IB, and IC, and in
two Dictyostelium myosin I isozymes that are putative substrates for the
kinase. Similar sequences do not occur in the myosins I from intestinal
brush border, which is not a substrate for the Acanthamoeba kinase.
Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides
Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
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