The Quaternary Organization and Dynamics of the Molecular Chaperone HSP26 Are Thermally Regulated
Benesch, Justin L. P.; Aquilina, John Andrew; Baldwin, Andrew J.; Rekas, Agata; Stengel, Florian; Lindner, Robin; Basha, Eman; Devlin, Glyn; Horwitz, Joseph; Vierling, Elizabeth; Carver, John; Robinson, Carol V.
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...[Show more]
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