The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated

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dc.contributor.authorBenesch, J.
dc.contributor.authorAquilina, J.
dc.contributor.authorBaldwin, A.
dc.contributor.authorRekas, A.
dc.contributor.authorStengel, F.
dc.contributor.authorLindner, R.
dc.contributor.authorBasha, E.
dc.contributor.authorDevlin, G.
dc.contributor.authorHorwitz, J.
dc.contributor.authorVierling, E.
dc.contributor.authorCarver, J.
dc.contributor.authorRobinson, C.
dc.date.issued2010
dc.description.abstractThe 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.
dc.description.statementofresponsibilityJustin 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
dc.description.urihttp://www.cell.com/chemistry-biology/home
dc.identifier.citationChemistry and Biology, 2010; 17(9):1008-1017
dc.identifier.doi10.1016/j.chembiol.2010.06.016
dc.identifier.issn1074-5521
dc.identifier.issn1879-1301
dc.identifier.urihttp://hdl.handle.net/2440/62734
dc.language.isoen
dc.publisherCell Press
dc.relation.grantNHMRC
dc.relation.grantARC
dc.rightsCopyright © 2010 Elsevier Ltd All rights reserved.
dc.source.urihttps://doi.org/10.1016/j.chembiol.2010.06.016
dc.subjectSaccharomyces cerevisiae Proteins
dc.subjectHeat-Shock Proteins
dc.subjectChromatography, Gel
dc.subjectSpectrometry, Fluorescence
dc.subjectNuclear Magnetic Resonance, Biomolecular
dc.subjectSpectrometry, Mass, Electrospray Ionization
dc.subjectTemperature
dc.subjectProtein Structure, Quaternary
dc.subjectLight
dc.subjectScattering, Radiation
dc.titleThe quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated
dc.typeJournal article
pubs.publication-statusPublished

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