Plant Chimeric Ca2+/Calmodulin-dependent Protein Kinase

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Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain.

Calcium, a universal second messenger, regulates diverse cellular processes in eukaryotes. Ca2+ and Ca2+/calmodulin-regulated protein phosphorylation play a pivotal role in amplifying and diversifying the action of Ca(2+)-binding domain was cloned and characterized from lily. The cDNA clone contains an open reading frame coding for a protein of 520 amino acids. The predicted structure of CCaMK ...

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Calcium-stimulated autophosphorylation site of plant chimeric calcium/calmodulin-dependent protein kinase.

The existence of two molecular switches regulating plant chimeric Ca(2+)/calmodulin-dependent protein kinase (CCaMK), namely the C-terminal visinin-like domain acting as Ca(2+)-sensitive molecular switch and calmodulin binding domain acting as Ca(2+)-stimulated autophosphorylation-sensitive molecular switch, has been described (Sathyanarayanan, P. V., Cremo, C. R., and Poovaiah, B. W. (2000) J....

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Plant chimeric Ca2+/Calmodulin-dependent protein kinase. Role of the neural visinin-like domain in regulating autophosphorylation and calmodulin affinity.

Chimeric Ca(2+)/calmodulin-dependent protein kinase (CCaMK) is characterized by a serine-threonine kinase domain, an autoinhibitory domain, a calmodulin-binding domain and a neural visinin-like domain with three EF-hands. The neural visinin-like Ca(2+)-binding domain at the C-terminal end of the CaM-binding domain makes CCaMK unique among all the known calmodulin-dependent kinases. Biological f...

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Plant Chimeric Ca/Calmodulin-dependent Protein Kinase ROLE OF THE NEURAL VISININ-LIKE DOMAIN IN REGULATING AUTOPHOSPHORYLATION AND CALMODULIN AFFINITY*

Chimeric Ca/calmodulin-dependent protein kinase (CCaMK) is characterized by a serine-threonine kinase domain, an autoinhibitory domain, a calmodulin-binding domain and a neural visinin-like domain with three EF-hands. The neural visinin-like Ca-binding domain at the C-terminal end of the CaM-binding domain makes CCaMK unique among all the known calmodulindependent kinases. Biological functions ...

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THE EFFECT OF THEOPHYLLINE ON THE KINETICS OF cAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT, cAMP, PROTEIN KINASE INHIBITOR AND THEIR RELATIONSHIP IN LUNG TISSUE

We have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. The results show that the point of highest concentration of the C subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 Ilg/ InL and 10µg/mL theophylline, this is shifted to I.S an...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2000

ISSN: 0021-9258

DOI: 10.1074/jbc.m000771200