Abstract
By chemical cross-linking and analytical ultracentrifugation the dimer is shown to be the predominant quaternary structure of HBsu, the major histone-like protein from Bacillus subtilis, at protein concentrations up to 1 mM. At low ionic strength between 0 and 100 mM Nacl, higher-order structures up to the hexamer are also found. A double-stranded 10-basepair DNA oligomer is demonstrated to prevent the aggregation of HBsu molecules as does an increase in ionic strength. The complex formed between HBsu and the DNA decamer is determined to consist of two protein dimers and the DNA. The association constant is about 106 M−1.
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© 1995 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG
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Timmermann, C., Behlke, J., Ristau, O., Gerst, H., Heinemann, U. (1995). Chemical cross-linking and analytical ultracentrifugation study of the histone-like protein HBsu: Quaternary structure and DNA binding. In: Behlke, J. (eds) Analytical Ultracentrifugation. Progress in Colloid & Polymer Science, vol 99. Steinkopff. https://doi.org/10.1007/BFb0114073
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DOI: https://doi.org/10.1007/BFb0114073
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