ArticleThe Journal of biological chemistry2014
Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 75 citations in OpenAlex.
- Comparative genomic and evolutionary analysis of the heat shock protein gene family in the chicken genome.Animal biotechnology · 2026Article
- Isolation and genomic characterization of Bacillus X32: a potent phosphate-solubilizing bacterium with growth-promoting effects on navel orange seedlings.Archives of microbiology · 2026Article
- Article
- Full-Length Transcriptome Sequencing and hsp Gene Family Analysis Provide New Insights into the Stress Response Mechanisms ofBiology · 2025Article
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- Domain Architecture Based Methods for Comparative Functional Genomics Toward Therapeutic Drug Target Discovery.Journal of molecular evolution · 2023Review
- J-domain Proteins form Binary Complexes with Hsp90 and Ternary Complexes with Hsp90 and Hsp70.Journal of molecular biology · 2023Article
- HtpG Is a Metal-Dependent Chaperone Which Assists the DnaK/DnaJ/GrpE Chaperone System of Mycobacterium tuberculosis via Direct Association with DnaJ2.Microbiology spectrum · 2023Article
- Uncoupling the Hsp90 and DnaK chaperone activities revealed the in vivo relevance of their collaboration in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Physiological and muscle tissue responses inFrontiers in physiology · 2022Article
- The Hsp70-Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration.Cellular and molecular life sciences : CMLS · 2021Review
- Visualizing Borrelia burgdorferi Infection Using a Small-Molecule Imaging Probe.Journal of clinical microbiology · 2021Article
- Structural Communication between theInternational journal of molecular sciences · 2021Article
- Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates.Frontiers in molecular biosciences · 2021Article
- The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation.Nature communications · 2020Article
- DnaK3 Is Involved in Biogenesis and/or Maintenance of Thylakoid Membrane Protein Complexes in the CyanobacteriumLife (Basel, Switzerland) · 2020Article
- Intermolecular Interactions between Hsp90 and Hsp70.Journal of molecular biology · 2019Article
- Hsp90 ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Quantitative Analyses Reveal Novel Roles formBio · 2019Article
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, heat shock protein 90 (Hsp90) is an essential ATP-dependent molecular chaperone that associates with numerous client proteins. HtpG, a prokaryotic homolog of Hsp90, is essential for thermotolerance in cyanobacteria, and in vitro it suppresses the aggregation of denatured proteins efficiently. Understanding how the non-native client proteins bound to HtpG refold is of central importance to comprehend the essential role of HtpG under stress. Here, we demonstrate by yeast two-hybrid method, immunoprecipitation assays, and surface plasmon resonance techniques that HtpG physically interacts with DnaJ2 and DnaK2. DnaJ2, which belongs to the type II J-protein family, bound DnaK2 or HtpG with submicromolar affinity, and HtpG bound DnaK2 with micromolar affinity. Not only DnaJ2 but also HtpG enhanced the ATP hydrolysis by DnaK2. Although assisted by the DnaK2 chaperone system, HtpG enhanced native refolding of urea-denatured lactate dehydrogenase and heat-denatured glucose-6-phosphate dehydrogenase. HtpG did not substitute for DnaJ2 or GrpE in the DnaK2-assisted refolding of the denatured substrates. The heat-denatured malate dehydrogenase that did not refold by the assistance of the DnaK2 chaperone system alone was trapped by HtpG first and then transferred to DnaK2 where it refolded. Dissociation of substrates from HtpG was either ATP-dependent or -independent depending on the substrate, indicating the presence of two mechanisms of cooperative action between the HtpG and the DnaK2 chaperone system.
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