ArticleJournal of molecular biology2013
An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Molecular Equilibrist: The Small Heat Shock Protein IbpA from Mycoplasma.Biomolecules · 2026Article
- A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain.Protein science : a publication of the Protein Society · 2023Review
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Transcriptomic and Physiological Response of Durum Wheat Grain to Short-Term Heat Stress during Early Grain Filling.Plants (Basel, Switzerland) · 2021Article
- Multiple nanocages of a cyanophage small heat shock protein with icosahedral and octahedral symmetries.Scientific reports · 2021Article
- Genome-Wide Analysis of the HSP20 Gene Family and Expression Patterns ofFrontiers in genetics · 2021Article
- The Small Ones Matter-sHsps in the Bacterial Chaperone Network.Frontiers in molecular biosciences · 2021Review
- The Mitochondrial Small Heat Shock Protein HSP22 from Pea is a Thermosoluble Chaperone Prone to Co-Precipitate with Unfolding Client Proteins.International journal of molecular sciences · 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
- A Class II small heat shock protein OsHsp18.0 plays positive roles in both biotic and abiotic defense responses in rice.Scientific reports · 2017Article
- Role of sHsps in organizing cytosolic protein aggregation and disaggregation.Cell stress & chaperones · 2017Review
- Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding.The EMBO journal · 2017Article
- Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Nature communications · 2016Article
- Article
- A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Journal of molecular biology · 2015Review
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- Identification of multiple small heat-shock protein genes in Plutella xylostella (L.) and their expression profiles in response to abiotic stresses.Cell stress & chaperones · 2015Article
- The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Dissecting the functional role of the N-terminal domain of the human small heat shock protein HSPB6.PloS one · 2014Article
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 3 countries.
Funding
Abstract
Small heat shock proteins (sHSPs) are virtually ubiquitous stress proteins that are also found in many normal tissues and accumulate in diseases of protein folding. They generally act as ATP-independent chaperones to bind and stabilize denaturing proteins that can be later reactivated by ATP-dependent Hsp70/DnaK, but the mechanism of substrate capture by sHSPs remains poorly understood. A majority of sHSPs form large oligomers, a property that has been linked to their effective chaperone action. We describe AtHsp18.5 from Arabidopsis thaliana, demonstrating that it is dimeric and exhibits robust chaperone activity, which adds support to the model that suboligomeric sHSP forms are a substrate binding species. Notably, like oligomeric sHSPs, when bound to substrate, AtHsp18.5 assembles into large complexes, indicating that reformation of sHSP oligomeric contacts is not required for assembly of sHSP-substrate complexes. Monomers of AtHsp18.5 freely exchange between dimers but fail to coassemble in vitro with dodecameric plant cytosolic sHSPs, suggesting that AtHsp18.5 does not interact by coassembly with these other sHSPs in vivo. Data from controlled proteolysis and hydrogen-deuterium exchange coupled with mass spectrometry show that the N- and C-termini of AtHsp18.5 are highly accessible and lack stable secondary structure, most likely a requirement for substrate interaction. Chaperone activity of a series of AtHsp18.5 truncation mutants confirms that the N-terminal arm is required for substrate protection and that different substrates interact differently with the N-terminal arm. In total, these data imply that the core α-crystallin domain of the sHSPs is a platform for flexible arms that capture substrates to maintain their solubility.
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