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Published on: June 24, 2016
Ferguson Plot Analysis of Chaperone ClpB from Moderate Halophile
Teruo Akuta1, Yui Tomioka1, Tomoto Ura2,3
1Research and Development Division, Kyokuto Pharmaceutical Industrial Co., Ltd, 3333-26, Aza-Asayama, Kamitezuna Tahahagi, Ibaraki, 318-0004, Japan.
Abstract:
The Ferguson plot is a simple method for determining the molecular weight of native proteins and their complexes. In this study, we tested the validity of the Ferguson plot based on agarose native gel electrophoresis using multimeric chaperone protein, ClpB, derived from a moderate halophile that forms a native hexamer. The Ferguson plot showed a single band with a molecular weight of 1,500 kDa, approximately twice the size of the native hexamer. This result is consistent with the structure of other chaperons that form a double ring assembly comprising two hexameric units, i.e., a dodecamer. Supporting this, dynamic light scattering experiment showed two peaks, which likely correspond to the hexamer and dodecamer structures.

