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Type: Journal article
Title: The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated
Author: Benesch, J.
Aquilina, J.
Baldwin, A.
Rekas, A.
Stengel, F.
Lindner, R.
Basha, E.
Devlin, G.
Horwitz, J.
Vierling, E.
Carver, J.
Robinson, C.
Citation: Chemistry and Biology, 2010; 17(9):1008-1017
Publisher: Cell Press
Issue Date: 2010
ISSN: 1074-5521
Statement of
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
Protein Structure, Quaternary
Scattering, Radiation
Rights: Copyright © 2010 Elsevier Ltd All rights reserved.
DOI: 10.1016/j.chembiol.2010.06.016
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Chemistry publications
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