Quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated

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dc.contributor.authorBenesch, JLPen_AU
dc.contributor.authorAquilina, JAen_AU
dc.contributor.authorBaldwin, AJen_AU
dc.contributor.authorRekas, Aen_AU
dc.contributor.authorStengel, Fen_AU
dc.contributor.authorLindner, RAen_AU
dc.contributor.authorBasha, Een_AU
dc.contributor.authorDevlin, GLen_AU
dc.contributor.authorHorwitz, Jen_AU
dc.contributor.authorVierling, Een_AU
dc.contributor.authorCarver, JAen_AU
dc.contributor.authorRobinson, CVen_AU
dc.date.accessioned2010-11-08T22:38:00Zen_AU
dc.date.available2010-11-08T22:38:00Zen_AU
dc.date.issued2010-09-24en_AU
dc.date.statistics2010-09-24en_AU
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. © 2010, Elsevier Ltd.en_AU
dc.identifier.citationBenesch, J. L. P., Aquilina, J. A., Baldwin, A. J., Rekas, A. Stengel, F., Lindner, R. A., Basha, E., Devlin, G. L., Horwits, J., Vierling, E., Carver, J. A., & Robinson, C. V. (2010). Quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated. Chemistry & Biology, 17(9), 1008-1017. doi:10.1016/j.chembiol.2010.06.016en_AU
dc.identifier.govdoc3042en_AU
dc.identifier.issn1074-5521en_AU
dc.identifier.issue9en_AU
dc.identifier.journaltitleChemistry & Biologyen_AU
dc.identifier.pagination1008-1017en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.chembiol.2010.06.016en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2842en_AU
dc.identifier.volume17en_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.subjectHeat-shock proteinsen_AU
dc.subjectLight scatteringen_AU
dc.subjectFluorescence spectroscopyen_AU
dc.subjectMass spectroscopyen_AU
dc.subjectThermalizationen_AU
dc.subjectMoleculesen_AU
dc.titleQuaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulateden_AU
dc.typeJournal Articleen_AU
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