ArticleJournal of molecular biology2014
Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Phosphorylation-Driven Epichaperome Assembly: A Critical Regulator of Cellular Adaptability and Proliferation.Research square · 2024Article
- Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Inhibitors of theCells · 2021Review
- Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates.Frontiers in molecular biosciences · 2021Article
- Allosteric Regulation of Rod Photoreceptor Phosphodiesterase 6 (PDE6) Elucidated by Chemical Cross-Linking and Quantitative Mass Spectrometry.Journal of molecular biology · 2019Article
- Different Grp94 components interact transiently with the myocilin olfactomedin domain in vitro to enhance or retard its amyloid aggregation.Scientific reports · 2019Article
- Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex.Nature communications · 2018Article
- Chemical cross-linking in the structural analysis of protein assemblies.Methods (San Diego, Calif.) · 2018Review
- The molecular architecture of the yeast spindle pole body core determined by Bayesian integrative modeling.Molecular biology of the cell · 2017Article
- Methods of probing the interactions between small molecules and disordered proteins.Cellular and molecular life sciences : CMLS · 2017Review
- Metadynamic metainference: Enhanced sampling of the metainference ensemble using metadynamics.Scientific reports · 2016Article
- Automated structure modeling of large protein assemblies using crosslinks as distance restraints.Nature methods · 2016Article
- Molecular Dynamics Simulations Reveal the Mechanisms of Allosteric Activation of Hsp90 by Designed Ligands.Scientific reports · 2016Article
- Bacterial Heat Shock Protein Activity.Journal of clinical and diagnostic research : JCDR · 2016Review
- Metainference: A Bayesian inference method for heterogeneous systems.Science advances · 2016Article
- The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling.Nature communications · 2015Article
- A systematic survey of an intragenic epistatic landscape.Molecular biology and evolution · 2015Article
- Determining protein complex structures based on a Bayesian model of in vivo Förster resonance energy transfer (FRET) data.Molecular & cellular proteomics : MCP · 2014Article
- Characterization of the Grp94/OS-9 chaperone-lectin complex.Journal of molecular biology · 2014Article
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Authors and funding
8 authors.
Funding
Abstract
Hsp90 is a conformationally dynamic molecular chaperone known to promote the folding and activation of a broad array of protein substrates ("clients"). Hsp90 is believed to preferentially interact with partially folded substrates, and it has been hypothesized that the chaperone can significantly alter substrate structure as a mechanism to alter the substrate functional state. However, critically testing the mechanism of substrate recognition and remodeling by Hsp90 has been challenging. Using a partially folded protein as a model system, we find that the bacterial Hsp90 adapts its conformation to the substrate, forming a binding site that spans the middle and C-terminal domains of the chaperone. Cross-linking and NMR measurements indicate that Hsp90 binds to a large partially folded region of the substrate and significantly alters both its local and long-range structure. These findings implicate Hsp90's conformational dynamics in its ability to bind and remodel partially folded proteins. Moreover, native-state hydrogen exchange indicates that Hsp90 can also interact with partially folded states only transiently populated from within a thermodynamically stable, native-state ensemble. These results suggest a general mechanism by which Hsp90 can recognize and remodel native proteins by binding and remodeling partially folded states that are transiently sampled from within the native ensemble.
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