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J. Biol. Chem., Vol. 261, Issue 26, 12166-12171, Sep, 1986
DB Glass, HC Cheng, BE Kemp and DA Walsh
Synthetic peptides corresponding to the active domain of the heat- stable
inhibitor protein of cAMP-dependent protein kinase (Cheng, H.- C., Kemp, B.
E., Pearson, R. B., Smith, A. J., Misconi, L., Van Patten, S. M., and
Walsh, D. A. (1986) J. Biol. Chem. 261, 989-992) were tested as inhibitors
of cGMP-dependent protein kinase. The peptides themselves were not
substrates. cGMP-dependent protein kinase activity was assayed using
histone H2B and two synthetic peptide substrates. Consistent with previous
observations of other peptide inhibitors of this enzyme (Glass, D. B.
(1983) Biochem. J. 213, 159-164), the inhibitory peptides had no effect on
the phosphorylation of histone H2B, but they competitively inhibited
cGMP-dependent phosphorylation of the two peptide substrates. The parent
inhibitor peptide, PKI(5-24)amide, and a series of analogs had Ki (or IC50)
values for cGMP-dependent protein kinase in the range of 15-190 microM. In
contrast to their effects on the cAMP-dependent protein kinase, the
inhibitory peptides were substantially less potent with cGMP-dependent
protein kinase, and potency was reduced by the presence of the NH2-terminal
residues (residues 5-13). We conclude that the two protein kinases share a
recognition of the basic amino acid cluster within the pseudosubstrate
region of the peptide, but that the cGMP-dependent protein kinase does not
recognize additional NH2-terminal determinants that make the inhibitor
protein extremely potent toward the cAMP-dependent enzyme. Even- when
tested at high concentrations and with peptide substrates, the native
inhibitor protein did not inhibit cGMP-dependent protein kinase under assay
conditions in which the peptides derived from it were inhibitory. Thus, the
native inhibitor protein appears to have structural features which block
interaction with the cGMP-dependent enzyme and enhance its selectivity for
cAMP-dependent protein kinase.
Differential and common recognition of the catalytic sites of the cGMP- dependent and cAMP-dependent protein kinases by inhibitory peptides derived from the heat-stable inhibitor protein
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