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Senescence-induced changes in autophosphorylation status and catalytic activity of plasma membrane protein kinases in soybean primary leaves

Wang Ningning, Wang Yong, Zhang Zili, Zhu Liangji, Zhang Ren

Department of Biochemistry and Molecular Biology,Nankai University.Tianjin 300071；Australia

Abstract

The results suggested that there were multiple sites on a 57 kD calcium-dependent protein kinase (CDPK) molecule for autophosphorylation and that autophosphorylation could improve its catalytic activity in phosphorylating histone H1. ST-induced changes in in vivo autophosphorylation status of the 57 kD CDPK may play an important role in regulating its catalytic activity during leaf senescence, and 6-BA pretreatment may make the high catalytic activity of this kinase longlasting. The effect of 6-BA application on ST-induced changes of autophosphorylation activity of a 39 kD and a 47 kD protein kinases implied involvement of these two kinases in cytokinin stimulus/response cascade system.

Key words: Soybean;Leaf;Cytokinin;Protein kinase;Au-tophosphorylation

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Citing This Article：

Wang Ningning, Wang Yong, Zhang Zili, Zhu Liangji, Zhang Ren. Senescence-induced changes in autophosphorylation status and catalytic activity of plasma membrane protein kinases in soybean primary leaves. Acta Physiol Sin 2001; 53 (1): (in Chinese with English abstract).