Low Resolution Structure of RAR1-GST-Tag Fusion Protein in Solution |
| M. Taubea, A. Jarmołowskib and M. Kozaka
a Department of Macromolecular Physics, Faculty of Physics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland b Department of Gene Expression, Institute of Molecular Biology and Biotechnology, Faculty of Biology, A. Mickiewicz University, Umultowska 89, 61-614 Poznań, Poland |
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| RAR1 is a protein required for resistance mediated by many R genes and function upstream of signaling pathways leading to H2O2 accumulation. The structure and conformation of RAR1-GST-Tag fusion protein from barley (Hordeum vulgare) in solution was studied by the small angle scattering of synchrotron radiation. It was found that the dimer of RAR1-GST-Tag protein is characterized in solution by radius of gyration RG = 6.19 nm and maximal intramolecular vector Dmax = 23 nm. On the basis of the small angle scattering of synchrotron radiation SAXS data two bead models obtained by ab initio modeling are proposed. Both models show elongated conformations. We also concluded that molecules of fusion protein form: dimers in solution via interaction of GST domains. |
| DOI: 10.12693/APhysPolA.117.307 PACS numbers: 61.05.cf, 87.14.E-, 87.14.et |