ArticleChemistry & biology2010
The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.
Article in Chemistry & biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins.The Biochemical journal · 2025Article
- The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins.Cell stress & chaperones · 2023Review
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Nature communications · 2021Article
- Linking the dynamics of chromatin occupancy and transcription with predictive models.Genome research · 2021Article
- The Small Ones Matter-sHsps in the Bacterial Chaperone Network.Frontiers in molecular biosciences · 2021Review
- The multifaceted nature of αB-crystallin.Cell stress & chaperones · 2020Review
- Conditional Disorder in Small Heat-shock Proteins.Journal of molecular biology · 2020Article
- Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates.PLoS genetics · 2019Article
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- MetaUniDec: High-Throughput Deconvolution of Native Mass Spectra.Journal of the American Society for Mass Spectrometry · 2019Article
- Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.Frontiers in pharmacology · 2019Review
- It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.The Journal of biological chemistry · 2018Article
- Self-assembly of toroidal proteins explored using native mass spectrometry.Chemical science · 2018Article
- The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.Cell stress & chaperones · 2017Article
- Proline isomerization in the C-terminal region of HSP27.Cell stress & chaperones · 2017Article
- The growing world of small heat shock proteins: from structure to functions.Cell stress & chaperones · 2017Review
- Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding.The EMBO journal · 2017Article
- Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure.PloS one · 2017Article
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Authors and funding
12 authors.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.