ArticleNature chemical biology2018
Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 119 citations in OpenAlex.
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- Complex compositional and metabolic response of river sediment microbiomes to multiple anthropogenic stressors.ISME communications · 2026Article
- Photothermal therapy triggering organelle stress and metabolic reprogramming to potentiate antitumor immunity.Frontiers in immunology · 2026Review
- Mechanisms of assembly and function of the Hsp70-Hsp40 chaperone machinery.Molecular cell · 2025Article
- Transcriptional Condensates: Epigenetic Reprogramming and Therapeutic Targets in Hematologic Malignancies.Cancers · 2025Review
- Single-molecule study of the dynamics of the molecular chaperone Hsp70 during the functional cycle.Biochemical Society transactions · 2025Review
- Exploring Yeast's Energy Dynamics: The General Stress Response Lowers Maintenance Energy Requirement.Microbial biotechnology · 2025Article
- Stochastic thermodynamics for biological functions.Quantitative biology (Beijing, China) · 2025Review
- An outmoded in vitro-inferred mechanism for chaperonin-accelerated protein refolding is confirmed in cells by cryo-electron tomography.Cell stress & chaperones · 2024Article
- Dissipative Self-Assembly of Patchy Particles under Nonequilibrium Drive: A Computational Study.Journal of chemical theory and computation · 2024Article
- Chaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis.PLoS biology · 2024Article
- Article
- Chaperones vs. oxidative stress in the pathobiology of ischemic stroke.Frontiers in molecular neuroscience · 2024Review
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- The Time-Resolved Salt Stress Response ofInternational journal of molecular sciences · 2023Article
- Maize heat shock proteins-prospection, validation, categorization and in silico analysis of the different ZmHSP families.Stress biology · 2023Article
- Design of an Arabidopsis thaliana reporter line to detect heat-sensing and signaling mutants.Plant methods · 2023Article
- A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70.Nature chemical biology · 2023Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During and after protein translation, molecular chaperones require ATP hydrolysis to favor the native folding of their substrates and, under stress, to avoid aggregation and revert misfolding. Why do some chaperones need ATP, and what are the consequences of the energy contributed by the ATPase cycle? Here, we used biochemical assays and physical modeling to show that the bacterial chaperones GroEL (Hsp60) and DnaK (Hsp70) both use part of the energy from ATP hydrolysis to restore the native state of their substrates, even under denaturing conditions in which the native state is thermodynamically unstable. Consistently with thermodynamics, upon exhaustion of ATP, the metastable native chaperone products spontaneously revert to their equilibrium non-native states. In the presence of ATPase chaperones, some proteins may thus behave as open ATP-driven, nonequilibrium systems whose fate is only partially determined by equilibrium thermodynamics.
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