TAILIEUCHUNG - Báo cáo khoa học: Amino acid residues on the surface of soybean 4-kDa peptide involved in the interaction with its binding protein

Soybean 4-kDa peptide, a hormone-like peptide, is a ligand for the 43-kDaprotein in legumes that functions as aprotein kinase and controls cell proliferation and differentiation. As this peptide stimulates proteinkinase activity, the interaction between the 4-kDa peptide (leginsulin) and the 43-kDa protein is considered important for signal transduction. However, the mechanism of interaction between the 4-kDa peptide and the 43-kDa protein is not clearly understood. | Eur. J. Biochem. 270 2583-2592 2003 FEBS 2003 doi Amino acid residues on the surface of soybean 4-kDa peptide involved in the interaction with its binding protein Kazuki Hanada1 Yuji Nishiuchi2 and Hisashi Hirano1 1 Yokohama City University Kihara Institute for Biological ResearchỊGraduate School of Integrated Science Yokohama Japan 2Peptide Institute Inc. Protein Research Foundation Osaka Japan Soybean 4-kDa peptide a hormone-like peptide is a ligand for the 43-kDa protein in legumes that functions as a protein kinase and controls cell proliferation and differentiation. As this peptide stimulates protein kinase activity the interaction between the 4-kDa peptide leginsulin and the 43-kDa protein is considered important for signal transduction. However the mechanism of interaction between the 4-kDa peptide and the 43-kDa protein is not clearly understood. We therefore investigated the binding mechanism between the 4-kDa peptide and the 43-kDa protein by using gelfiltration chromatography and dot-blot immunoanalysis and found that the 4-kDa peptide bound to the dimer form of the 43-kDa protein. Surface plasmon resonance analysis was then used to explore the interaction between the 4-kDa peptide and the 43-kDa protein. To identify the residues of the 4-kDa peptide involved in the interaction with the 43-kDa protein alanine-scanning mutagenesis of the 4-kDa peptide was performed. The 4-kDa peptide-expression system in Escherichia coli which has the ability to install disulfide bonds into the target protein in the cytoplasm was employed to produce the 4-kDa peptide and its variants. Using mass spectrometry the expressed peptides were confirmed as the oxidized forms of the native peptide. Surface plasmon resonance analysis showed that the C-terminal hydrophobic area of the 4-kDa peptide plays an important role in binding to the 43-kDa protein. Keywords hormone-like peptide receptor-like protein protein-protein interaction alanine-scanning

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