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KMID : 0368419920350010085
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Journal of Plant Biology
1992 Volume.35 No. 1 p.85 ~ p.90
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Identification of Proteins Phosphorylated by Protein Kinase C in Soybean
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崔允僖/Choy, Yoon Hi
許圭晶/李埈承/Hur, Kyu Chung/Lee, June Seung
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Abstract
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The previous report (Chung and Lee, 1992) in our laboratory demonstrated that the protein kinase C(PKC) activator, TPA, promotes the elongation of corn coleoptiles significantly. To understand the role of TPA on the growth, substrates of PKC were investigated using PKC partially purified from soybean by DEAE-52 cellulose column. The enzyme activity increased about 5-fold in the presence of Ca^2+, phosphatidylserine and diolein compared with that in the absence of these reagents. Phosphorylation of both cytosol and membrane proteins by the purified PKC increased in the presence of Ca^2+ compared with that of EGTA treatment. However, the phosphorylation did not increase markedly by treatment with TPA of phosphatidylserine and diolein in the presence of Ca^2+ compared with Ca^2+ alone. The decrease in phosphorylation of 100, 61 and 43 Kd proteins of the cytosol, and 140, 11, 66, 47 and 32 Kd membrane proteins in hypocotyls, and 140, 110, 66, 47, 33, 31 and 16 Kd membrane proteins in the root was observed in the presence of PKC inhibitor staurosporine (STA). These results suggest that subatrates of PKC in soybean may be 110, 63 and 41 Kd proteins of the cytosol, and 140, 110, 66, 47 and 32 Kd membrane proteins in the subapical region of the hypocotyl, and 140, 110, 66, 47, 33, 31 and 16 Kd membrane proteins of the root.
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