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Mechanism of the activation of proteinase inhibitor synthesis by systemin involves β-sheet structure, a specific DNA-binding protein domain

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Slósarek,  Genowefa
Max Planck Institute for Medical Research, Max Planck Society;

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Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Slósarek, G., Kalbitzer, H. R., Mucha, P., Rekowski, P., Kupryszewski, G., Giel-Pietraszuk, M., et al. (1995). Mechanism of the activation of proteinase inhibitor synthesis by systemin involves β-sheet structure, a specific DNA-binding protein domain. Journal of Structural Biology, 115(1), 30-36. doi:10.1006/jsbi.1995.1026.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-4FE0-1
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-β-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 gone expression and thus explain the biological activity of systemin.