Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated|
|Citation:||Chemistry & Biology, 2010; 17(9):1008-1017|
|Justin L.P. Benesch, J. Andrew Aquilina, Andrew J. Baldwin, Agata Rekas, Florian Stengel, Robyn A. Lindner, Eman Basha, Glyn L. Devlin, Joseph Horwitz, Elizabeth Vierling, John A. Carver, and Carol V. Robinson|
|Abstract:||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.|
|Keywords:||Saccharomyces cerevisiae Proteins; Heat-Shock Proteins; Chromatography, Gel; Spectrometry, Fluorescence; Nuclear Magnetic Resonance, Biomolecular; Spectrometry, Mass, Electrospray Ionization; Temperature; Protein Structure, Quaternary; Light; Scattering, Radiation|
|Rights:||Copyright © 2010 Elsevier Ltd All rights reserved.|
|Appears in Collections:||Chemistry publications|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.