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Title: Mechanism of the activation of proteinase inhibitor synthesis by systemin involves beta-sheet structure, a specific DNA-binding protein domain. Author: Slósarek G, Kalbitzer HR, Mucha P, Rekowski P, Kupryszewski G, Giel-Pietraszuk M, Szymański M, Barciszewski J. Journal: J Struct Biol; 1995; 115(1):30-6. PubMed ID: 7577230. Abstract: We analyzed a tertiary structure of systemin, the first identified polypeptide plant hormone, using two-dimensional NMR spectroscopy. From these data and molecular dynamics calculations we concluded that the peptide can adopt a Z-like-beta-sheet structure, which has previously been found in many specific DNA-binding proteins. Using DNA-cellulose affinity chromatography, we showed that systemin binds strongly to DNA. We suggest that the specific systemin-DNA interaction, particularly in a promoter region of the proteinase inhibitors, could effect gene expression and thus explain the biological activity of systemin.[Abstract] [Full Text] [Related] [New Search]