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Plant and Cell Physiology, 2000, Vol. 41, No. 11 1243-1250
© 2000 Oxford University Press

Involvement of Calcium-Dependent Protein Kinase in Rice (Oryza sativa L.) Lamina Inclination Caused by Brassinolide

Guangxiao Yang and Setsuko Komatsu1

Department of Molecular Genetics, National Institute of Agrobiological Resources, Tsukuba, 305-8602 Japan

Promotive effect of brassinolide (BL) on green lamina inclination was concentration-dependent when excised rice (Oryza sativa L.) lamina was floated on BL solution under continuous light conditions. Protein kinase inhibitor staurosporine and Ca2+ channel blocker LaCl3 could completely, while Ca2+ chelator EGTA could partially inhibit the lamina inclination caused by BL. Two protein kinases with apparent molecular masses of 45 and 54 kDa were detected using an in-gel kinase assay with histone III-S as a substrate. In particular, the changes in 45 kDa protein kinase activity correlated with lamina inclination caused by BL. The 45 kDa kinase activity was inhibited by Ca2+ chelator EGTA, protein kinase inhibitor, staurosporine and calmodulin antagonist W-7. Therefore, this 45 kDa protein kinase was identified as a Ca2+-dependent protein kinase (CDPK). Patterns of 2-dimensional PAGE after in vitro phosphorylation of crude extracts showed that the phosphorylation of 56 and 41 kDa proteins, which was Ca2+ -dependent, was strongly increased by BL treatment. These results suggested that CDPK and Ca2+-dependent protein phosphorylation are involved in BL-induced rice lamina inclination.

1 Corresponding author: E-mail, skomatsu@abr.affrc.go.jp; Fax, +81-298-38-7408; Phone, +81-298-38-7446.


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