ArticleThe Journal of biological chemistry2010
Mechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 91 citations in OpenAlex.
- Responses of grapevine cells to physiological doses of ethanol, including induced resistance to heat stress.Plant biology (Stuttgart, Germany) · 2025Article
- Molecular chaperone function of three small heat-shock proteins from a model probiotic species.Cell stress & chaperones · 2023Article
- Comparative Transcriptome Profiling of Cassava Tuberous Roots in Response to Postharvest Physiological Deterioration.International journal of molecular sciences · 2022Article
- Elucidation of Diverse Physico-Chemical Parameters in Mammalian Small Heat Shock Proteins: A Comprehensive Classification and Structural and Functional Exploration Using In Silico Approach.Applied biochemistry and biotechnology · 2021Article
- Glycinebetaine mitigated the photoinhibition of photosystem II at high temperature in transgenic tomato plants.Photosynthesis research · 2021Article
- Regulation of small heat-shock proteins by hetero-oligomer formation.The Journal of biological chemistry · 2020Article
- 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
- Silencing of class I small heat shock proteins affects seed-related attributes and thermotolerance in rice seedlings.Planta · 2019Article
- 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
- Article
- It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.The Journal of biological chemistry · 2018Article
- Over-expression of chrysanthemum CmDREB6 enhanced tolerance of chrysanthemum to heat stress.BMC plant biology · 2018Article
- Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions.Science (New York, N.Y.) · 2018Article
- The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles.Drug design, development and therapy · 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
- Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.The Journal of biological chemistry · 2017Article
- Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure.PloS one · 2017Article
- Class I and II Small Heat Shock Proteins Together with HSP101 Protect Protein Translation Factors during Heat Stress.Plant physiology · 2016Article
- Reversible thermal unfolding of a yfdX protein with chaperone-like activity.Scientific reports · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The small heat shock proteins (sHSPs) and alpha-crystallins are highly effective, ATP-independent chaperones that can bind denaturing client proteins to prevent their irreversible aggregation. One model of sHSP function suggests that the oligomeric sHSPs are activated to the client-binding form by dissociation at elevated temperatures to dimers or other sub-oligomeric species. Here we examine this model in a comparison of the oligomeric structure and chaperone activity of two conserved classes of cytosolic sHSPs in plants, the class I (CI) and class II (CII) proteins. Like the CI sHSPs, recombinant CII sHSPs from three divergent plant species, pea, wheat, and Arabidopsis, are dodecamers as determined by nano-electrospray mass spectrometry. While at 35 to 45 degrees C, all three CI sHSPs reversibly dissociate to dimers, the CII sHSPs retain oligomeric structure at high temperature. The CII dodecamers are, however, dynamic and rapidly exchange subunits, but unlike CI sHSPs, the exchange unit appears larger than a dimer. Differences in dodecameric structure are also reflected in the fact that the CII proteins do not hetero-oligomerize with CI sHSPs. Binding of the hydrophobic probe bis-ANS and limited proteolysis demonstrate CII proteins undergo significant, reversible structural changes at high temperature. All three recombinant CII proteins more efficiently protect firefly luciferase from insolubilization during heating than do the CI proteins. The CI and CII proteins behave strictly additively in client protection. In total, the results demonstrate that different sHSPs can achieve effective protection of client proteins by varied mechanisms.
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