MECHANISM OF THE ACTIVATION OF PROTEINASE INHIBITOR SYNTHESIS BY SYSTEMIN INVOLVES BETA-SHEET STRUCTURE, A SPECIFIC DNA-BINDING PROTEIN DOMAIN

摘要

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. (C) 1995 Academic Press, Inc. [References: 33]