ArticlePlant physiology2000
A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein.
Article in Plant physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
128 citing papers in PubMed, 451 citations in OpenAlex.
- Stress granules at the crossroads of the proteostasis network.RNA biology · 2026Review
- A small heat shock protein from Arabidopsis thaliana regulates glyceraldehyde-3-phosphate dehydrogenase in the drought tolerance.Plant cell reports · 2026Article
- Article
- How does protein aggregate structure affect mechanisms of disaggregation?Biochemical Society transactions · 2025Review
- Mechanism of small heat shock protein client sequestration and induced polydispersity.Nature communications · 2025Article
- The Effect of Heat Stress on Wheat Flag Leaves Revealed by Metabolome and Transcriptome Analyses During the Reproductive Stage.International journal of molecular sciences · 2025Article
- Article
- Novel Strategy for In Vitro Validation of Babesia orientalis Heat Shock Proteins Chaperone Activity and Thermostability.Acta parasitologica · 2024Article
- Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana.Journal of experimental botany · 2023Article
- Construction of heat stress regulation networks based on Illumina and SMRT sequencing data in potato.Frontiers in plant science · 2023Article
- Genomic Survey of Heat Shock Proteins inInternational journal of molecular sciences · 2022Article
- Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen PhosphorylaseInternational journal of molecular sciences · 2022Article
- Comparative transcriptome analysis of heat stress responses of Clematis lanuginosa and Clematis crassifolia.BMC plant biology · 2022Article
- Genome-Wide Analysis of HSP70s in Hexaploid Wheat: Tandem Duplication, Heat Response, and Regulation.Cells · 2022Article
- Response of Tomato (Plants (Basel, Switzerland) · 2022Article
- Minimal Yet Powerful: The Role of Archaeal Small Heat Shock Proteins in Maintaining Protein Homeostasis.Frontiers in molecular biosciences · 2022Review
- A novel transcription factor CmMYB012 inhibits flavone and anthocyanin biosynthesis in response to high temperatures in chrysanthemum.Horticulture research · 2021Article
- The Caenorhabditis elegans 12-kDa small heat shock proteins with little in vitro chaperone activity play crucial roles for its dauer formation, longevity, and reproduction.Protein science : a publication of the Protein Society · 2021Article
- The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70.Scientific reports · 2021Article
- Advances in Understanding of Desiccation Tolerance of Lichens and Lichen-Forming Algae.Plants (Basel, Switzerland) · 2021Review
68 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Small heat shock proteins (sHsps) are a diverse group of heat-induced proteins that are conserved in prokaryotes and eukaryotes and are especially abundant in plants. Recent in vitro data indicate that sHsps act as molecular chaperones to prevent thermal aggregation of proteins by binding non-native intermediates, which can then be refolded in an ATP-dependent fashion by other chaperones. We used heat-denatured firefly luciferase (Luc) bound to pea (Pisum sativum) Hsp18.1 as a model to define the minimum chaperone system required for refolding of a sHsp-bound substrate. Heat-denatured Luc bound to Hsp18.1 was effectively refolded either with Hsc/Hsp70 from diverse eukaryotes plus the DnaJ homologs Hdj1 and Ydj1 (maximum = 97% Luc reactivation with k(ob) = 1.0 x 10(-2)/min), or with prokaryotic Escherichia coli DnaK plus DnaJ and GrpE (100% Luc reactivation, k(ob) = 11.3 x 10(-2)/min). Furthermore, we show that Hsp18.1 is more effective in preventing Luc thermal aggregation than the Hsc70 or DnaK systems, and that Hsp18.1 enhances the yields of refolded Luc even when other chaperones are present during heat inactivation. These findings integrate the aggregation-preventive activity of sHsps with the protein-folding activity of the Hsp70 system and define an in vitro system for further investigation of the mechanism of sHsp action.
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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.