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The function of ScHSP26 is thermally controlled: the heat shock that causes the destabilization of target proteins leads to its activation as a molecular chaperone. We investigate the structural and dynamical properties of ScHSP26 oligomers through a combination of multiangle light scattering, fluorescence spectroscopy, NMR spectroscopy, and mass spectrometry. We show that ScHSP26 exists as a heterogeneous oligomeric ensemble at room temperature. At heat-shock temperatures, two shifts in equilibria are observed: toward dissociation and to larger oligomers. We examine the quaternary dynamics of these oligomers by investigating the rate of exchange of subunits between them and find that this not only increases with temperature but proceeds via two separate processes. This is consistent with a conformational change of the oligomers at elevated temperatures which regulates the disassembly rates of this thermally activated protein.

Original publication

DOI

10.1016/j.chembiol.2010.06.016

Type

Journal article

Journal

Chem Biol

Publication Date

24/09/2010

Volume

17

Pages

1008 - 1017

Keywords

Chromatography, Gel, Heat-Shock Proteins, Light, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Quaternary, Saccharomyces cerevisiae Proteins, Scattering, Radiation, Spectrometry, Fluorescence, Spectrometry, Mass, Electrospray Ionization, Temperature