Calmodulin isoform-specific activation of a rice calmodulin-binding kinase conferred by only three amino-acids of OsCaM61
| Autor: | Lei Zhang, Dian-Fan Li, Ying-Tang Lu, Li Ma, Jing Li |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Tryptophane intrinsic fluorescence
Molecular Sequence Data Glycine Biophysics Electrophoretic Mobility Shift Assay Dissociation constant Mitogen-activated protein kinase kinase Biology Calmodulin-binding protein kinase Biochemistry MAP2K7 Calmodulin Structural Biology Ca2+/calmodulin-dependent protein kinase Serine Genetics Protein Isoforms Amino Acid Sequence Calmodulin isoform-specific activation Kinase activity Molecular Biology Serine/threonine-specific protein kinase Alanine MAP kinase kinase kinase food and beverages Oryza Cell Biology Enzyme Activation Spectrometry Fluorescence Calcium-Calmodulin-Dependent Protein Kinases Mutation Calcium Cyclin-dependent kinase 9 Casein kinase 2 Sequence Alignment |
| Zdroj: | FEBS Letters. (18):4325-4331 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2006.06.090 |
| Popis: | The kinase activity of a Ca(2+)/calmodulin (CaM)-binding serine/threonine protein kinase from rice (Oryza sativa) (OsCBK) has been reported to be unaffected by OsCaM1 binding. In this study, we examined whether other rice CaMs can stimulate OsCBK. It was observed that OsCaM61 stimulated OsCBK in a Ca(2+)-dependent manner. In addition, Ala(111), Gly(123) and Ser(127) were identified as critical residues for OsCBK activation. Mutational study and fluorescent spectroscopy analysis indicated that CaM-binding affinity does not correlate with the kinase activity and that these key amino-acids in OsCaM61 play a vital role in suitable changes of OsCBK conformation for kinase activation. |
| Databáze: | OpenAIRE |
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