ArticleProceedings of the National Academy of Sciences of the United States of America2001
Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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86 citing papers in PubMed, 283 citations in OpenAlex.
- Review
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- Impact of heat stress on physiological characteristics and expression of heat shock proteins (HSPs) in groundnut (Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
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- The role of membrane physiology in sHSP Lo18-lipid interaction and lipochaperone activity.Scientific reports · 2024Article
- Significant influence of four highly conserved amino-acids in lipochaperon-active sHsps on the structure and functions of the Lo18 protein.Scientific reports · 2023Article
- Insight into the biochemical and cell biological function of an intrinsically unstructured heat shock protein, Hsp12 of Ustilago maydis.Molecular plant pathology · 2023Article
- Design of an Arabidopsis thaliana reporter line to detect heat-sensing and signaling mutants.Plant methods · 2023Article
- Differential Accumulation of sHSPs Isoforms during Desiccation of the Resurrection PlantLife (Basel, Switzerland) · 2023Article
- Molecular chaperone function of three small heat-shock proteins from a model probiotic species.Cell stress & chaperones · 2023Article
- The Common Bean Small Heat Shock Protein Nodulin 22 fromMolecules (Basel, Switzerland) · 2022Article
- The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes.International journal of molecular sciences · 2022Article
- Physio-anatomical modifications and elemental allocation pattern in Acanthus ilicifolius L. subjected to zinc stress.PloS one · 2022Article
- Lipids and Trehalose Actively Cooperate in Heat Stress Management ofInternational journal of molecular sciences · 2021Article
- The Small Ones Matter-sHsps in the Bacterial Chaperone Network.Frontiers in molecular biosciences · 2021Review
- Multiple Functions of Spectrin: Convergent Effects.The Journal of membrane biology · 2020Review
- IbpB-bound substrate release in living cells as revealed by unnatural amino acid-mediated photo-crosslinking.FEBS open bio · 2020Article
- Small but mighty: a functional look at bacterial sHSPs.Cell stress & chaperones · 2020Review
26 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 6 institutions in 4 countries.
Funding
Abstract
The small heat shock proteins (sHSPs) are ubiquitous stress proteins proposed to act as molecular chaperones to prevent irreversible protein denaturation. We characterized the chaperone activity of Synechocystis HSP17 and found that it has not only protein-protective activity, but also a previously unrecognized ability to stabilize lipid membranes. Like other sHSPs, recombinant Synechocystis HSP17 formed stable complexes with denatured malate dehydrogenase and served as a reservoir for the unfolded substrate, transferring it to the DnaK/DnaJ/GrpE and GroEL/ES chaperone network for subsequent refolding. Large unilamellar vesicles made of synthetic and cyanobacterial lipids were found to modulate this refolding process. Investigation of HSP17-lipid interactions revealed a preference for the liquid crystalline phase and resulted in an elevated physical order in model lipid membranes. Direct evidence for the participation of HSP17 in the control of thylakoid membrane physical state in vivo was gained by examining an hsp17(-) deletion mutant compared with the isogenic wild-type hsp17(+) revertant Synechocystis cells. We suggest that, together with GroEL, HSP17 behaves as an amphitropic protein and plays a dual role. Depending on its membrane or cytosolic location, it may function as a "membrane stabilizing factor" as well as a member of a multichaperone protein-folding network. Membrane association of sHSPs could antagonize the heat-induced hyperfluidization of specific membrane domains and thereby serve to preserve structural and functional integrity of biomembranes.
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