Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051822 | FEBS Letters | 2006 | 7 Pages |
Abstract
The kinase activity of a Ca2+/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 Ca2+-dependent manner. In addition, Ala111, Gly123 and Ser127 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.
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Plant Science
Authors
Dian-Fan Li, Jing Li, Li Ma, Lei Zhang, Ying-Tang Lu,