Intermolecular Interactions between Hsp90 and Hsp70
Open accessAbstract
Members of the Hsp90 and Hsp70 families of molecular chaperones are imp\ortant for the maintenance of protein homeostasis and cellular recovery following environmental stresses, such as heat and oxidative stress. Moreover, the two chaperones can collaborate in protein remodeling and activation. In higher eukaryotes, Hsp90 and Hsp70 form a functionally active complex with Hop (Hsp90-Hsp70 organizing protein) acting as a bridge between the two chaperones. In bacteria, which do not contain a Hop homolog, Hsp90 and Hsp70, DnaK, directly interact during protein remodeling. Although yeast possesses a Hop-like protein, Sti1, Hsp90, and Hsp70 can directly interact in yeast in the absence of Sti1. Previous studies showed that residues in the middle domain of Escherichia coli Hsp90 are important for interaction with the J-protein binding region of DnaK. The results did not distinguish between the possibility that (i) these sites were involved in direct interaction and (ii) the residues in these sites participate in conformational changes which are transduced to other sites on Hsp90 and DnaK that are involved in the direct interaction. Here we show by crosslinking experiments that the direct interaction is between a site in the middle domain of Hsp90 and the J-protein binding site of Hsp70 in both E. coli and yeast. Moreover, J-protein promotes the Hsp70-Hsp90 interaction in the presence of ATP, likely by converting Hsp70 into the ADP-bound conformation. The identification of the protein-protein interaction site is anticipated to lead to a better understanding of the collaboration between the two chaperones in protein remodeling.
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Mutations at interface I on Hsp90 (G333, K414, K418, K419) or Hsp70 (R171, N174, D213) cause defective Hsp90-Hsp70 interaction, growth defects, and impaired maturation of GR, v-Src and luciferase.
“This explains why mutations at interface I on either Hsp90 (G333, K414, K418, K419)21–23 or Hsp70 (R171, N174, D213)24 led to defective Hsp90-Hsp70 interaction, growth defects and impaired client maturation of GR, v-Src and luciferase (Fig. 1d, e, Extended Data Fig. 4c–h; see Supplementary Table 3 for equivalent yeast residue numbering).”
From Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism (2022) · cites this paper as [24]
The citation is attached to the Hsp70 residues, not the Hsp90 residues cited to other papers. In the Results section on Ssa1 substitution mutants (page unavailable), the source reports that yeast Hsp70 mutants R169H, N172D and E210R had reduced interaction with Hsp82 and were defective in reactivating heat-denatured luciferase. It does not establish growth defects or impaired GR and v-Src maturation, and the passage does not verify the citing sentence’s residue numbering. (LLM, conf=0.86)
Experimental — accuracy not yet measuredSequence alignments show that interface I and II residues are generally conserved among Hsp90 and Hsp70 homologues and paralogues, suggesting a universal Hsp90-Hsp70 binding strategy across species and organelles.
“Finally, sequence alignments of Hsp90 and Hsp70 homologues and paralogues showed that interface I and II residues are generally conserved, suggesting a universal Hsp90–Hsp70 binding strategy across species23,24,27 and organelles28,29 (Supplementary Fig. 2a, b).”
From Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism (2022) · cites this paper as [24]
The Results section reports that direct Hsp90–Hsp70 interaction sites are conserved between bacteria and yeast. It does not report sequence alignments showing general conservation of interface I and II residues across homologues and paralogues, or establish a universal binding strategy across species and organelles. The Discussion describes conservation in higher eukaryotes as only possible; page numbers are unavailable in our copy. (LLM, conf=0.85)
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Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism
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Self-citation
- Authors
- Doyle, S. M., Hoskins, J. R., Kravats, A. N., Heffner, A. L., Garikapati, S., & Wickner, S.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Doyle, Shannon M.
- Wickner, Sue
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2019-07
- Volume
- 431
- Issue
- 15
- Pages
- 2729-2746
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC6599576
- OpenAlex
- W2944868387
- Cited by
- 64
- References
- 74
- Citations by year
- 2026: 5 · 2025: 13 · 2024: 10 · 2023: 9 · 2022: 6 · 2021: 15 · 2020: 4 · 2019: 2
- FWCI
- 2.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Intramural Research Program
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- HSP90, HSP70, protein-protein interaction, DnaK, STI1, Humulus lupulus, molecular chaperones, protein remodeling, ATP binding, Escherichia coli, yeast, crosslinking
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Escherichia coli, Models, Molecular, Saccharomyces cerevisiae, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Saccharomyces cerevisiae Proteins, Escherichia coli Proteins, Protein Interaction Domains and Motifs, Protein Interaction Maps
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