Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling
Open accessAbstract
Hsp90 is a highly conserved molecular chaperone that remodels hundreds of client proteins, many involved in the progression of cancer and other diseases. It functions with the Hsp70 chaperone and numerous cochaperones. The bacterial Hsp90 functions with an Hsp70 chaperone, DnaK, but is independent of Hsp90 cochaperones. We explored the collaboration between Escherichia coli Hsp90 and DnaK and found that the two chaperones form a complex that is stabilized by client protein binding. A J-domain protein, CbpA, facilitates assembly of the Hsp90Ec-DnaK-client complex. We identified E. coli Hsp90 mutants defective in DnaK interaction in vivo and show that the purified mutant proteins are defective in physical and functional interaction with DnaK. Understanding how Hsp90 and Hsp70 collaborate in protein remodeling will provide the groundwork for the development of new therapeutic strategies targeting multiple chaperones and cochaperones.
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Interface II defines the Hsp90ATP-like position and orientation of the Hsp90NTD relative to the Hsp90MD, explaining why Hsp70 accelerates Hsp90 ATPase activity.
“Notably, interface II defines the Hsp90ATP-like position and orientation of the Hsp90NTD with respect to the Hsp90MD, explaining the observation that Hsp70 accelerates Hsp90 ATPase activity25.”
From Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism (2022) · cites this paper as [25]
The Results section (“ATP hydrolysis by Hsp90Ec and DnaK is synergistically stimulated”; page not provided) reports enhanced ATP hydrolysis by the two chaperones together in the presence of the client protein L2. It does not establish that Hsp70 specifically accelerates Hsp90’s ATPase, and the cited paper does not describe interface II positioning the Hsp90 N-terminal domain relative to its middle domain or propose that positioning as the explanation. (LLM, conf=0.86)
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MethodInfluentialInterplay between E. coli DnaK, ClpB and GrpE during Protein Disaggregation
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“Similarly, a DnaKmutant, T199A, which can bind but not hydrolyze ATP [37], was biotinylated and found to bind Hsp90Ec more weakly than a similarly biotinylated wild-type DnaK in the presence of L2 and CbpA (Fig.”
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“However, when cells carry mutations in Hsp90Ec they grow more slowly at high temperature [20], exhibit a slight increase in aggregated proteins at high temperature [21], lose adaptive immunity conferred by the CRISPR system [22] and show a subtle defect in motility [23].”
Background
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Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540 · see citing works
Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling
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“Additionally, the mutants were defective in protein remodeling in collaboration with DnaK, showing that the Hsp90Ec–DnaK interaction is important for functional collaboration (11).”
BackgroundResultInfluentialSelf-citationStructure, Function, and Regulation of the Hsp90 MachineryPreprint
Biebl, M. M., & Büchner, J. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034017 · Cited by 308 · see citing works
“Interestingly, direct contacts between Hsp90 and Hsp70 have been reported in bacteria, which lack cochaperones, and also in yeast, suggesting that a direct transfer is also possible (Genest et al. 2015; Kravats et al. 2018).”
BackgroundStructure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism
Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04252-1 · Cited by 213 · see citing works
How Do J-Proteins Get Hsp70 to Do So Many Different Things?
Craig, E. A., & Marszałek, J. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.02.007 · Cited by 197 · see citing works
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BackgroundHsp90 Breaks the Deadlock of the Hsp70 Chaperone System
Luengo, T. M., Kityk, R., Mayer, M. P., & Rüdiger, S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.028 · Cited by 151 · see citing works
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The Plasticity of the Hsp90 Co-chaperone System
Sahasrabudhe, P., Rohrberg, J., Biebl, M. M., Rutz, D. A., & Buchner, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.004 · Cited by 136 · see citing works
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BackgroundFunctional and physical interaction between yeast Hsp90 and Hsp70
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“Due to the homology between Ssa1 and DnaK, the region on Ssa1 that interacts with Hsp82 may also be involved in interactions with Hsp40 and with the Ssa1 substratebinding domain, as has been observed for the homologous region of DnaK (46–50).”
BackgroundInfluentialSelf-citationDynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes
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BackgroundFunctional principles and regulation of molecular chaperones
Dahiya, V., & Büchner, J. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.10.001 · Cited by 75 · see citing works
Bhattacharya, K., & Picard, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03962-z · Cited by 73 · see citing works
Intermolecular Interactions between Hsp90 and Hsp70
Doyle, S. M., Hoskins, J. R., Kravats, A. N., Heffner, A. L., Garikapati, S., & Wickner, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.026 · Cited by 64 · see citing works
“Our previous mutagenesis studies, both in vivo and in vitro, as well as molecular modeling showed that residues in the middle domain of Hsp90Ec are important for interaction with DnaK [32, 38] and residues in the DnaJ binding region on DnaK are important for the interaction with Hsp90Ec [32].”
BackgroundInfluentialSelf-citationIdentification of induced mutations in hexaploid wheat genome using exome capture assay
Hussain, M., Iqbal, M. A., Till, B. J., & Rahman, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201918 · Cited by 60 · see citing works
Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis
Honoré, F. A., Méjean, V., & Genest, O. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.082 · Cited by 59 · see citing works
“Two-hybrid plasmids were transformed in the Bth101DhtpG strain (Genest et al., 2015).”
BackgroundSelf-citationThe interactions of molecular chaperones with client proteins: why are they so weak?
Arhar, T., Shkedi, A., Nadel, C. M., & Gestwicki, J. E. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101282 · Cited by 55 · see citing works
Hsp70-mediated quality control: should I stay or should I go?
Kohler, V., & Andréasson, C. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0187 · Cited by 57 · see citing works
NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems
Biebl, M. M., Delhommel, F., Faust, O., Żak, K. M., Agam, G. N., Guo, X., Mühlhofer, M., Dahiya, V., Hillebrand, D., Popowicz, G. M., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.12.031 · Cited by 48 · see citing works
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Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK
Kravats, A. N., Doyle, S. M., Hoskins, J. R., Genest, O., Doody, E. E., & Wickner, S. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.12.014 · Cited by 46 · see citing works
“galactosidase compared to coexpression of T25-DnaK wild-type and T18-vector [30]”
BackgroundMethodResultInfluentialSelf-citationJohnston, C. L., Marzano, N. R., van Oijen, A. M., & Ecroyd, H. W. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.021 · Cited by 45 · see citing works
The Bacterial Hsp90 Chaperone: Cellular Functions and Mechanism of Action
Wickner, S., Nguyen, T.-L. L., & Genest, O. (2021) · Annual Review of Microbiology · doi:10.1146/annurev-micro-032421-035644 · Cited by 40 · see citing works
Self-citationSun, M., Kotler, J. L. M., Liu, S., & Street, T. O. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007050 · Cited by 38 · see citing works
“Similar mutations disrupt coordination between the yeast cytosolic Hsp70/Hsp90 pair (15), suggesting that the location of this direct interaction between Hsp70 and Hsp90 may be widely conserved.”
BackgroundInfluentialGeneral Structural and Functional Features of Molecular Chaperones
Edkins, A. L., & Boshoff, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-78397-6_2 · Cited by 34 · see citing works
Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii
Zhang, Y., Launay, H. M. M., Schramm, A., Lebrun, R., & Gontero, B. (2018) · Scientific Reports · doi:10.1038/s41598-018-24772-7 · Cited by 34 · see citing works
Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates
Fauvet, B., Finka, A., Castanié‐Cornet, M., Cirinesi, A.-M., Genevaux, P., Quadroni, M., & Goloubinoff, P. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.653073 · Cited by 28 · see citing works
“Moreover, the collaboration between Hsp70 and Hsp90 has also been demonstrated in other organisms, such as yeast (Genest et al., 2013) and metazoans (Genest et al., 2018; Moran Luengo et al., 2018), where Hsp70/Hsp90 interactions are key to the maturation of the steroid hormone receptor (Li et al.,…”
BackgroundMolecular mechanisms of chaperone‐directed protein folding: Insights from atomistic simulations
Castelli, M., Magni, A., Bonollo, G., Pavoni, S., Frigerio, F., Oliveira, A. S. F., Cinquini, F., Serapian, S. A., & Colombo, G. (2023) · Protein Science · doi:10.1002/pro.4880 · Cited by 27 · see citing works
“Focusing on the dynamics of the client protein, GR's unfolded tail is rigidly coordinated with Hsp70C SBD and with Hsp90 M-Domain /Hsp90 CTD of both protomers (particularly with protomer B).”
BackgroundInfluentialAstl, L., & Verkhivker, G. M. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b01045 · Cited by 26 · see citing works
Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle
Reidy, M., Kumar, S., Anderson, D. E., & Masison, D. C. (2018) · Genetics · doi:10.1534/genetics.118.301178 · Cited by 22 · see citing works
Hsp90, a team player in protein quality control and the stress response in bacteria
Wickramaratne, A. C., Wickner, S., & Kravats, A. N. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00176-22 · Cited by 23 · see citing works
“The interaction is weak, in the low micromolar range (117, 123, 188), and is stabilized by a client protein (117) and a JDP (117–120).”
BackgroundResultInfluentialSelf-citationEl‐Kashef, D. H., Youssef, M. E., Nasr, M. H. A., Alrouji, M., Alhajlah, S. H., AlOmeir, O., Khalaf, N. E. A., Ghaffar, D. M. A., Jamil, L., Abdel-Nasser, Z. M., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113487 · Cited by 23 · see citing works
Structural transitions modulate the chaperone activities of Grp94
Amankwah, Y. S., Fleifil, Y., Unruh, E., Collins, P., Wang, Y., Vitou, K., Bates, A., Obaseki, I., Sugoor, M., Alao, J. P., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2309326121 · Cited by 22 · see citing works
“Grp94 directly interacts with BiP in vitro using homologous residues of Hsp90 and Hsp70 important for formation of the Hsp90 - Hsp70 complex in cytosolic systems (22, 23).”
Self-citationMakumire, S., Zininga, T., Vahokoski, J., Kursula, I., & Shonhai, A. (2020) · PLoS ONE · doi:10.1371/journal.pone.0226657 · Cited by 20 · see citing works
“coli lacks a Hop homolog [15] and the same protein is not essential in yeast [16], it has been reported to play an important role in the development of Trypanosoma cruzi and Trypanosoma brucei parasites [17].”
BackgroundMangla, N., Singh, R., & Agarwal, N. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.00312-23 · Cited by 20 · see citing works
“Earlier in vitro studies indicate that HSP70 first recognizes denatured luciferase, which is then transferred to HSP82 (Hsp90 homolog) via its connection with Sti1 (61), which bridges HSP82 and HSP70 during this process.”
BackgroundInfluentialRegulation of Age-Related Protein Toxicity
Pras, A., & Nollen, E. A. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.637084 · Cited by 22 · see citing works
Grp94 Works Upstream of BiP in Protein Remodeling Under Heat Stress
Amankwah, Y. S., Collins, P., Fleifil, Y., Unruh, E., Márquez, K. J. R., Vitou, K., & Kravats, A. N. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167762 · Cited by 19 · see citing works
Self-citationJ-domain Proteins form Binary Complexes with Hsp90 and Ternary Complexes with Hsp90 and Hsp70
Wickramaratne, A. C., Liao, J. R., Doyle, S. M., Hoskins, J. R., Puller, G. C., Scott, M. L., Alao, J. P., Obaseki, I., Dinan, J. C., Maity, T. K., et al. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168184 · Cited by 19 · see citing works
Self-citationHow soluble misfolded proteins bypass chaperones at the molecular level
Halder, R., Nissley, D. A., Sitarik, I. M., Jiang, Y., Rao, Y., Vu, Q. V., Li, M. S., Pritchard, J. R., & O’Brien, E. P. (2023) · Nature Communications · doi:10.1038/s41467-023-38962-z · Cited by 18 · see citing works
“Some experiments were performed in triplicate suggesting random experimental errors, such GroEL Client protein GroEL Fig.1|Meta-analysisofproteinrefoldingstudiesandrepresentationsofGroEL, DnaK, HtpG, and client proteins. a Through a meta-analysis of the experimental literature we fi nd an appreciable fraction (indicate…”
InfluentialDevelopment of a microarray-based assay for efficient testing of new HSP70/DnaK inhibitors
Mohammadi‐Ostad‐Kalayeh, S., Hrupins, V., Helmsen, S., Ahlbrecht, C., Stahl, F., Scheper, T. H., Preller, M., Surup, F., Stadler, M., Kirschning, A., et al. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.10.003 · Cited by 18 · see citing works
Jin, Y., Kotler, J. L. M., Wang, S., Huang, B., Halpin, J. C., & Street, T. O. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166963 · Cited by 17 · see citing works
Orchestration of algal metabolism by protein disorder
Launay, H., Receveur-Bréchot, V., Carrière, F., & Gontero, B. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108070 · Cited by 16 · see citing works
Hsp70/Hsp90 Organising Protein (Hop): Coordinating Much More than Chaperones
Schwarz, K., Baindur‐Hudson, S., Blatch, G. L., & Edkins, A. L. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-14740-1_3 · Cited by 13 · see citing works
Corteggiani, M., Bossuet‐Greif, N., Nougayrède, J., Byrne, D., Ilbert, M., Dementin, S., Giudici‐Orticoni, M., Méjean, V., Oswald, É., & Genest, O. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201779119 · Cited by 14 · see citing works
“In parallel, many biochemical studies have been performed to characterize the in vitro chaperone activity of E. coli Hsp90 (Hsp90 Ec ) (38, 39, 41, 57).”
InfluentialSelf-citationUpdate on the Protein Homeostasis Network in Bacillus subtilis
Matavacas, J., & von Wachenfeldt, C. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.865141 · Cited by 13 · see citing works
“For instance, apart from DnaK, E. coli harbors two additional Hsp70 proteins – Hsc66 (Seaton and Vickery, 1994) and Hsc62 (Yoshimune et al., 1998) – and five additional DnaJ-like proteins such as Hsc20 and CbpA (Ueguchi et al., 1994; Lelivelt and Kawula, 1995; Clarke et al., 1996; Itoh et al., 1999; Yoshimune et al.,…”
Choudhary, D., Mediani, L., Avellaneda, M. J., Bjarnason, S., Alberti, S., Boczek, E. E., Heidarsson, P. O., Mossa, A., Carra, S., Tans, S. J., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c02022 · Cited by 13 · see citing works
Hsp90 sensitivity to ADP reveals hidden regulation mechanisms
Halpin, J., & Street, T. O. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.08.005 · Cited by 11 · see citing works
“HtpG can interact directly with DnaK (a bacterial Hsp70 homolog), resulting in enhanced activation from L2 [8].”
BackgroundResultInfluentialStructural Communication between the E. coli Chaperones DnaK and Hsp90
Grindle, M. P., Carter, B., Alao, J. P., Connors, K., Tehver, R., & Kravats, A. N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042200 · Cited by 10 · see citing works
“The residues of DnaK and Hsp90Ec that are involved in the direct interaction have previously been described [65,66,72].”
BackgroundSelf-citationStudying heat shock proteins through single-molecule mechanical manipulation
Choudhary, D., Mediani, L., Carra, S., & Cecconi, C. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01096-y · Cited by 8 · see citing works
“2009); alternatively, they enabled to demonstrate the cooperation between chaperones such as HSP70 and HSP90 and how, at the molecular level, this is stabilised by the binding of the substrate, enabling its transfer from one chaperone to another (Genest et al. 2015).”
BackgroundKirschke, E., Roe-Zurz, Z., Noddings, C., & Agard, D. (2020) · doi:10.1101/2020.05.03.075523 · Cited by 6 · see citing works
Jiang, Z., Lu, J., Tong, Y., Yang, H., & Feng, S. (2023) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-023-03613-4 · Cited by 7 · see citing works
“(Genest et al. 2015).”
Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2020) · doi:10.1101/2020.11.05.370247 · Cited by 10 · see citing works
Hsp90, DnaK, and ClpB collaborate in protein reactivation
Hoskins, J. R., Wickramaratne, A. C., Jewell, C. P., Jenkins, L. M. M., & Wickner, S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2422640122 · Cited by 6 · see citing works
Self-citationConformational plasticity of a BiP–GRP94 chaperone complex
Brenner, J. C., Zirden, L. C., Buzuk, L., Almeida‐Hernández, Y., Radzuweit, L., Diamantino, J., Kaschani, F., Kaiser, M., Sánchez‐García, E., Poepsel, S., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01619-0 · Cited by 7 · see citing works
“ATP binding and hydrolysis of the BiP NBD regulate the conformation of the BiP SBD , with the ATP-bound open and the ADP-bound closed conformations representing the most extreme states (Fig.”
Transcriptomic Adaptation of Legionella pneumophila to Transient Heat Shock
Liang, J., & Faucher, S. P. (2022) · Frontiers in Water · doi:10.3389/frwa.2022.891477 · Cited by 6 · see citing works
Cytoplasmic molecular chaperones in Pseudomonas species
Kim, H., Moon, S., Ham, S., Lee, K., Römling, U., & Lee, C. D. (2022) · The Journal of Microbiology · doi:10.1007/s12275-022-2425-0 · Cited by 5 · see citing works
“The middle domain of Hsp90 interacts directly with DnaK in E. coli and substrate protein can be transferred from DnaK to Hsp90 for further processing (Genest et al., 2015, 2019).”
BackgroundKojima, R., Takai, S., Osada, H., Yamamoto, L., Furukawa, M., & Gullans, S. R. (2022) · Journal of Cell Science · doi:10.1242/jcs.258542 · Cited by 4 · see citing works
Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors
Azam, T. P., Han, J., Deans, E. E., Huang, B., Hoxie, R. S., Friedman, L. J., Gelles, J., & Street, T. O. (2025) · Nature Communications · doi:10.1038/s41467-025-58658-w · Cited by 3 · see citing works
“Inclient delivery,theHsp90dimerarmsareopen and Hsp70 can directly bind Hsp90 at “ interface I ” , which is conserved from E. coli 7,8 to yeast 9 to humans 10 and for Grp94 11 .”
Gollapalli, P., Rudrappa, S., Vadlapudi, K., & Kumar, H. S. S. (2023) · Journal of Molecular Evolution · doi:10.1007/s00239-023-10129-w · Cited by 2 · see citing works
“In E. coli and yeast, a portion of the MD interacts directly with Hsp70, and higher eukaryotes may also (Genest et al. 2015; Kra-vats et al. 2018).”
BackgroundHeterologous overexpression of Sup35 in Escherichia coli leads to both monomer and complex states
Wang, M., Wang, X. D., & Cheng, Z. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26327 · Cited by 2 · see citing works
Gaur, D., Kumar, N., Ghosh, A., Singh, P. R., Kumar, P., Guleria, J., Kaur, S., Malik, N., Saha, S., Nyström, T., et al. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010442 · Cited by 2 · see citing works
“Further, these direct interactions lead to synergistic stimulation of ATP hydrolysis activity and are required for client reactivation in vitro [20].”
BackgroundHoskins, J. R., Wickner, S., & Doyle, S. M. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7477-1_15 · Cited by 2 · see citing works
Self-citationFauvet, B., Finka, A., Castanié‐Cornet, M., Cirinesi, A.-M., Genevaux, P., Quadroni, M., & Goloubinoff, P. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/451989 · Cited by 2 · see citing works
Direct single-molecule visualization of Hsp90-mediated relief of an Hsp70-folding block
Marzano, N. R., Skewes, B., McMahon, S., Rice, L. J., Cox, D., van Oijen, A. M., & Ecroyd, H. W. (2026) · Science Advances · doi:10.1126/sciadv.aeg5464 · Cited by 1 · see citing works
“Among the most studied molecular chaperones are the intracellular heat shock proteins (Hsps), notably the Hsp70 and Hsp90 systems, which work cooperatively to guide polypeptides toward their native state ( 7 , 8 ).”
Sti1/Hop Plays a Pivotal Role in Hsp90 Regulation Beyond Bridging Hsp70
Reidy, M. J. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23158-3_17 · Cited by 1 · see citing works
Refolding activity of bacterial Hsp90 in vivo reveals ancient chaperoning functionPreprint
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“coli, and interestingly also in eukaryotic systems despite the presence of the linking co-chaperone Hop [37-40].”
BackgroundTargetomics, application of in vitro screening methods for the identification of new drugs
Mohammadi‐Ostad‐Kalayeh, S. (2018) · Institutional Repository of Leibniz Universität Hannover (Leibniz Universität Hannover) · doi:10.15488/3938
Garcie, C. (2016) · doi:10.70675/a730b904z2f56z4723z91deze0d7821e9847
“Ils ont poursuivi leur travaux en démontrant l’interaction directe entre DnaK et Hsp90Ec, dont la liaison est stabilisée par la formation du complexe [DnaK–Hsp90Ec–protéine cliente] [191].”
BackgroundDu, Y., Xia, S., Zhang, W., Yang, W., Yu, Y., Li, Z., Peng, B., Wang, Y., Liu, B., Tian, H., et al. (2026) · Fishes · doi:10.3390/fishes11050267
Adedeji, A., Unruh, E., Derr, A., Ndolo, C., Balch, M., Paul, K., Morton, A. J., & Kravats, A. N. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113358
“This functional partnership involves direct interactions between Hsp90 and Hsp70, with Hsp70 binding and stabilizing unfolded proteins before transfer to Hsp90 for final folding and activation (6, 44, 45).”
Self-citationProteostasis and ageing dissidence
Babu, N. L., Whalen, K. M., & Freeman, B. (2026) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2025.0266
“Hsp70 then hands off the elongated nascent chains to other chaperones, including TRiC and Hsp90, where more intricate folding topologies can be mediated, metastable forms maintained and/or subunits assembled into large biostructures [10 ,11 ] ( figure 1 ).”
- Authors
- Genest, O., Hoskins, J. R., Kravats, A. N., Doyle, S. M., & Wickner, S.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- National Institutes of Health (US)
- Corresponding author
- Doyle, Shannon M.
- Wickner, Sue
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2015-12
- Volume
- 427
- Issue
- 24
- Pages
- 3877-3889
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC4663108
- OpenAlex
- W2173310312
- Cited by
- 76
- References
- 55
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 2 · 2023: 7 · 2022: 12 · 2021: 9 · 2020: 8 · 2019: 6 · 2018: 12 · 2017: 7 · 2016: 5
- FWCI
- 3.47
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion)
- Funders
- National Institutes of Health, National Cancer Institute, Center for Cancer Research
- 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, DnaK, CbpA, J-domain, protein remodeling, Escherichia coli, co-chaperones
- MeSH terms
- Escherichia coli, Protein Binding, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Amino Acid Substitution, Escherichia coli Proteins, Protein Refolding
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