Slósarek, G. and Kalbitzer, Hans Robert and Mucha, P. and Rekowski, P. and Kupryszewski, G. and Giel-Pietraszuk, M. and Szymański, M. and Barciszewski, J. (1995) Mechanism of the activation of proteinase inhibitor synthesis by systemin involves beta-sheet structure, a specific DNA-binding protein domain. Journal of structural biology 115 (1), pp. 30-36.
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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.
|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Subjects:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited On:||09 Sep 2010 06:57|
|Last Modified:||09 Sep 2010 06:57|