Abstract
The E. coli heat shock proteins DnaK (Hsp70), DnaJ and GrpE constitute a cellular chaperone system for protein folding. In the context of a rigorous investigation of the structure-function relationships within this complex system we investigated the quaternary structure of DnaJ by analytical ultracentrifugation under conditions of sedimentation equilibrium. DnaJ appeared heterogeneous under all tested conditions. The observed heterogeneity depended mainly on the pH of the preparation. At pH 5.5 the sedimentation profiles were well fitted by two exponential functions, indicating the presence of a low and a high mole mass component. The distribution of the two components was independent of the protein concentration.
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© 1995 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG
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Schönfeld, HJ., Schmidt, D., Zulauf, M. (1995). Investigation of the molecular chaperone DnaJ by analytical ultracentrifugation. In: Behlke, J. (eds) Analytical Ultracentrifugation. Progress in Colloid & Polymer Science, vol 99. Steinkopff. https://doi.org/10.1007/BFb0114063
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DOI: https://doi.org/10.1007/BFb0114063
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