ArticleThe Journal of biological chemistry2013
Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding.
Article in The Journal of biological chemistry, 2013. 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, 49 citations in OpenAlex.
- A Study on the Temperature-Dependent Behavior of Small Heat Shock Proteins from Methanogens.International journal of molecular sciences · 2025Article
- Mechanism of small heat shock protein client sequestration and induced polydispersity.Nature communications · 2025Article
- Small Heat Shock Proteins: Protein Aggregation Amelioration and Neuro- and Age-Protective Roles.International journal of molecular sciences · 2025Review
- Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM.Nature communications · 2024Article
- Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM.bioRxiv : the preprint server for biology · 2024Article
- Chaperone regulation of biomolecular condensates.Frontiers in biophysics · 2024Article
- HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.International journal of molecular sciences · 2023Article
- Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation.Communications biology · 2023Article
- Multiple nanocages of a cyanophage small heat shock protein with icosahedral and octahedral symmetries.Scientific reports · 2021Article
- Advancements in protein nanoparticle vaccine platforms to combat infectious disease.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021Review
- 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
- Cryo-EM for Small Molecules Discovery, Design, Understanding, and Application.Cell chemical biology · 2018Review
- Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity.Structure (London, England : 1993) · 2018Article
- Loss of αB-crystallin function in zebrafish reveals critical roles in the development of the lens and stress resistance of the heart.The Journal of biological chemistry · 2018Article
- 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
- Multiple oligomeric structures of a bacterial small heat shock protein.Scientific reports · 2016Article
- The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.Nature structural & molecular biology · 2015Article
- Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.Biochemistry · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Small heat shock proteins (sHSPs) are ubiquitous chaperones that bind and sequester non-native proteins preventing their aggregation. Despite extensive studies of sHSPs chaperone activity, the location of the bound substrate within the sHSP oligomer has not been determined. In this paper, we used cryoelectron microscopy (cryoEM) to visualize destabilized mutants of T4 lysozyme (T4L) bound to engineered variants of the small heat shock protein Hsp16.5. In contrast to wild type Hsp16.5, binding of T4L to these variants does not induce oligomer heterogeneity enabling cryoEM analysis of the complexes. CryoEM image reconstruction reveals the sequestration of T4L in the interior of the Hsp16.5 oligomer primarily interacting with the buried N-terminal domain but also tethered by contacts with the α-crystallin domain shell. Analysis of Hsp16.5-WT/T4L complexes uncovers oligomer expansion as a requirement for high affinity binding. In contrast, a low affinity mode of binding is found to involve T4L binding on the outer surface of the oligomer bridging the formation of large complexes of Hsp16.5. These mechanistic principles were validated by cryoEM analysis of an expanded variant of Hsp16.5 in complex with T4L and Hsp16.5-R107G, which is equivalent to a mutant of human αB-crystallin linked to cardiomyopathy. In both cases, high affinity binding is found to involve conformational changes in the N-terminal region consistent with a central role of this region in substrate recognition.
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