ArticleThe Journal of biological chemistry2008
Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 81 citations in OpenAlex.
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- An experimental framework to assess biomolecular condensates in bacteria.Nature communications · 2024Article
- A review on oligomeric polydispersity and oligomers-dependent holding chaperone activity of the small heat-shock protein IbpB of Escherichia coli.Cell stress & chaperones · 2023Review
- Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process.Journal of the American Chemical Society · 2023Article
- An experimental framework to assess biomolecular condensates in bacteria.Research square · 2023Article
- An experimental framework to assess biomolecular condensates in bacteria.bioRxiv : the preprint server for biology · 2023Article
- Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition.Nature cell biology · 2022Article
- The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70.Scientific reports · 2021Article
- Structural basis of substrate recognition and thermal protection by a small heat shock protein.Nature communications · 2021Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates.PLoS genetics · 2019Article
- HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner.The Journal of biological chemistry · 2019Article
- Small heat shock proteins: multifaceted proteins with important implications for life.Cell stress & chaperones · 2019Article
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.The Journal of biological chemistry · 2018Article
- Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau.Nature communications · 2018Article
- Mapping interactions with the chaperone network reveals factors that protect against tau aggregation.Nature structural & molecular biology · 2018Article
- Role of sHsps in organizing cytosolic protein aggregation and disaggregation.Cell stress & chaperones · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Small heat shock proteins (sHSPs) and the related alpha-crystallins are ubiquitous chaperones linked to neurodegenerative diseases, myopathies, and cataract. To better define their mechanism of chaperone action, we used hydrogen/deuterium exchange and mass spectrometry (HXMS) to monitor conformational changes during complex formation between the structurally defined sHSPs, pea PsHsp18.1, and wheat TaHsp16.9, and the heat-denatured model substrates malate dehydrogenase (MDH) and firefly luciferase. Remarkably, we found that even when complexed with substrate, the highly dynamic local structure of the sHSPs, especially in the N-terminal arm (>70% exchange in 5 s), remains unchanged. These results, coupled with sHSP-substrate complex stability, indicate that sHSPs do not adopt new secondary structure when binding substrate and suggest sHSPs are tethered to substrate at multiple sites that are locally dynamic, a feature that likely facilitates recognition and refolding of sHSP-bound substrate by the Hsp70/DnaK chaperone system. Both substrates were found to be stabilized in a partially unfolded state that is observed only in the presence of sHSP. Furthermore, peptide-level HXMS showed MDH was substantially protected in two core regions (residues 95-156 and 228-252), which overlap with the MDH structure protected in the GroEL-bound MDH refolding intermediate. Significantly, despite differences in the size and structure of TaHsp16.9-MDH and PsHsp18.1-MDH complexes, peptide-level HXMS patterns for MDH in both complexes are virtually identical, indicating that stabilized MDH thermal unfolding intermediates are not determined by the identity of the sHSP.
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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.