PMID: 12787024Jun 6, 2003Paper

Amino acid residues on the surface of soybean 4-kDa peptide involved in the interaction with its binding protein

European Journal of Biochemistry
Kazuki HanadaH Hirano

Abstract

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 gel-filtration 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 ...Continue Reading

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Citations

Nov 19, 2004·Journal of Molecular Recognition : JMR·Rebecca L Rich, David G Myszka
Jul 28, 2010·The Journal of Biological Chemistry·Pedro Da SilvaFrédéric Gressent
Aug 12, 2010·Bioscience, Biotechnology, and Biochemistry·Andrei D ShutovNobuyuki Maruyama
Mar 8, 2008·Peptides·Xin-Peng DunZheng-Wang Chen
Feb 10, 2007·The FEBS Journal·Xin-Peng DunTomas Bergman
Feb 2, 2012·Toxins·Frédéric GressentCorinne Royer
Apr 2, 2021·Journal of Proteomics·Hisashi Hirano

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