Conformational properties of nuclear protein HMGB1 and specificity of its interaction with DNA |
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Authors: | A M Polyanichko T J Rodionova V I Vorob’ev E V Chikhirzhina |
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Institution: | 1.Department of Molecular Biophysics, Faculty of Physics,St. Petersburg State University,St. Petersburg,Russia;2.Institute of Cytology,Russian Academy of Sciences,St. Petersburg,Russia |
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Abstract: | Changes in secondary structure of DNA and non-histone chromosomal protein HMGB1 during the formation of the complex have been
studied by circular dichroism and UV spectroscopy. It was demonstrated that the HMGB1 protein is able to change its secondary
structure upon binding to DNA. Based on the assumption that there are two spectroscopically distinguishable forms of the HMGB1
in solution, we estimated the fraction of bound protein. The fraction of bound protein decreases at higher protein to DNA
ratios r from 0.48 at r = 0.13 to 0.06 at r = 2.43. It was shown that HMGB1 is able to induce considerable changes in DNA structure, even when the amount of protein
actually bound is low. |
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