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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Mechanism of the activation of proteinase inhibitor synthesis by systemin involves beta-sheet structure, a specific DNA-binding protein domain. Slósarek, G., Kalbitzer, H.R., Mucha, P., Rekowski, P., Kupryszewski, G., Giel-Pietraszuk, M., Szymański, M., Barciszewski, J. J. Struct. Biol. (1995) [Pubmed]
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