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KMID : 0380219930260020125
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 2 p.125 ~ p.131
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Characterization of a Ca2+/Calmodulin Dependent Phosphorylated Protein Expressed at the Early Stages of Soybean Germination
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Sang Yeol Lee
Jeong Dong Bahk/Jong Chan Hong and Moo Je Cho
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Abstract
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Using [γ-^(32)P] labelled ATP, an endogenous phosphorylated protein whose molecular weight was 52 kDa has been identified and characterized. It was rapidly appeared during the early stage of soybean germination. It was distinctively phosphorylated at the very early stages of cell growth and differentiation and slowly declined after 24 h. Therefore, the phosphorylated 52 kDa protein can be postulated to play significant roles in the control of embryonic cell growth and development. The 52 kDa phosphorylated protein was identified to be mainly located in the cytosolic fraction of soybean cell. Phosphorylation of this protein was dependent on Ca^(2+) and calmodulin but not on phospholipids. The requirement of free Ca^(2+) to phosphorylate this protein can be supplemented enough by soybean cell itself without the additions of Ca^(2+) from the external sources. The phospho-amino acids were identified as serine and threonine residues, which represented that the 52 kDa protein contained at least two phosphorylation sites.
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KEYWORD
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