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Calcium-stimulated Autophosphorylation Site of Plant Chimeric Calcium/Calmodulin-dependent Protein Kinase

Sathyanarayanan, P.V. ; Siems, William F. ; Jones, Jeffrey P. ; Poovaiah, B.W.

The Journal of biological chemistry, 2001-08, Vol.276 (35), p.32940-32947 [Periódico revisado por pares]

Legacy CDMS: Elsevier Inc

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Título:
Calcium-stimulated Autophosphorylation Site of Plant Chimeric Calcium/Calmodulin-dependent Protein Kinase
Autor: Sathyanarayanan, P.V. ; Siems, William F. ; Jones, Jeffrey P. ; Poovaiah, B.W.
Assuntos: Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites ; Calcium - metabolism ; Calcium - pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases - chemistry ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Chromatography, Affinity ; Kinetics ; Life Sciences (General) ; Liliaceae - enzymology ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptide Fragments - chemistry ; Peptide Fragments - isolation & purification ; Phosphopeptides - chemistry ; Phosphopeptides - isolation & purification ; Phosphorylation ; Protein Conformation ; Protein Structure, Secondary ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
É parte de: The Journal of biological chemistry, 2001-08, Vol.276 (35), p.32940-32947
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Descrição: The existence of two molecular switches regulating plant chimeric Ca2+/calmodulin-dependent protein kinase (CCaMK), namely the C-terminal visinin-like domain acting as Ca2+-sensitive molecular switch and calmodulin binding domain acting as Ca2+-stimulated autophosphorylation-sensitive molecular switch, has been described (Sathyanarayanan, P. V., Cremo, C. R., and Poovaiah, B. W. (2000) J. Biol. Chem. 275, 30417–30422). Here we report the identification of Ca2+-stimulated autophosphorylation site of CCaMK by matrix-assisted laser desorption ionization time of flight-mass spectrometry. Thr267 was confirmed as the Ca2+-stimulated autophosphorylation site by post-source decay experiments and by site-directed mutagenesis. The purified T267A mutant form of CCaMK did not show Ca2+-stimulated autophosphorylation, autophosphorylation-dependent variable calmodulin affinity, or Ca2+/calmodulin stimulation of kinase activity. Sequence comparison of CCaMK from monocotyledonous plant (lily) and dicotyledonous plant (tobacco) suggests that the autophosphorylation site is conserved. This is the first identification of a phosphorylation site specifically responding to activation by second messenger system (Ca2+ messenger system) in plants. Homology modeling of the kinase and calmodulin binding domain of CCaMK with the crystal structure of calcium/calmodulin-dependent protein kinase 1 suggests that the Ca2+-stimulated autophosphorylation site is located on the surface of the kinase and far from the catalytic site. Analysis of Ca2+-stimulated autophosphorylation with increasing concentration of CCaMK indicates the possibility that the Ca2+-stimulated phosphorylation occurs by an intermolecular mechanism.
Editor: Legacy CDMS: Elsevier Inc
Idioma: Inglês

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Calcium-stimulated Autophosphorylation Site of Plant Chimeric Calcium/Calmodulin-dependent Protein Kinase

Sathyanarayanan, P.V. ; Siems, William F. ; Jones, Jeffrey P. ; Poovaiah, B.W.

Legacy CDMS: Elsevier Inc

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