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231223s2006 xx ||||| 00| ||eng c |
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|a pubmed24n0545.xml
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|a (DE-627)NLM163425442
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|a (NLM)16765480
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Syam Prakash, S R
|e verfasserin
|4 aut
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|a Heterologous expression and biochemical characterization of two calcium-dependent protein kinase isoforms CaCPK1 and CaCPK2 from chickpea
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|c 2006
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
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|2 rdacarrier
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|a Date Completed 08.12.2006
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|a Date Revised 11.03.2022
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|a published: Print-Electronic
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|a GENBANK: AY312268, AY312269
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|a Citation Status MEDLINE
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|a In plants, calcium-dependent protein kinases (CPKs) constitute a unique family of enzymes consisting of a protein kinase catalytic domain fused to carboxy-terminal autoregulatory and calmodulin-like domains. We isolated two cDNAs encoding calcium-dependent protein kinase isoforms (CaCPK1 and CaCPK2) from chickpea. Both isoforms were expressed as fusion proteins in Escherichia coli. Biochemical analyses have identified CaCPK1 and CaCPK2 as Ca(2+)-dependent protein kinases since both enzymes phosphorylated themselves and histone III-S as substrate only in the presence of Ca(2+). The kinase activity of the recombinant enzymes was calmodulin independent and sensitive to CaM antagonists W7 [N-(6-aminohexyl)-5-chloro-1-naphthalene sulphonamide] and calmidazoilum. Phosphoamino acid analysis revealed that the isoforms transferred the gamma-phosphate of ATP only to serine residues of histone III-S and their autophosphorylation occurred on serine and threonine residues. These two isoforms showed considerable variations with respect to their biochemical and kinetic properties including Ca(2+) sensitivities. The recombinant CaCPK1 has a pH and temperature optimum of pH 6.8-8.6 and 35-42 degrees C, respectively, whereas CaCPK2 has a pH and temperature optimum of pH 7.2-9 and 35-42 degrees C, respectively. Taken together, our results suggest that CaCPK1 and CaCPK2 are functional serine/threonine kinases and may play different roles in Ca(2+)-mediated signaling in chickpea plants
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Calmodulin
|2 NLM
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|a Isoenzymes
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Recombinant Proteins
|2 NLM
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|a Protein Kinases
|2 NLM
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|a EC 2.7.-
|2 NLM
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|a Jayabaskaran, Chelliah
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 163(2006), 11 vom: 28. Nov., Seite 1083-93
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
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|g volume:163
|g year:2006
|g number:11
|g day:28
|g month:11
|g pages:1083-93
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|a AR
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|d 163
|j 2006
|e 11
|b 28
|c 11
|h 1083-93
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