ArticleThe Journal of biological chemistry2020
An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Development of domain-specific probes ofAntimicrobial agents and chemotherapy · 2026Article
- In silico identification of selective cyclodecapeptide inhibitors targeting Plasmodium falciparum Grp78 chaperone.Journal of computer-aided molecular design · 2026Article
- Biochemical and biophysical characterization of Plasmodium falciparum glucose regulated protein 170.Scientific reports · 2025Article
- Advances in the structures, mechanisms and targeting of molecular chaperones.Signal transduction and targeted therapy · 2025Review
- Cellular protection from HCell stress & chaperones · 2023Article
- The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response.Archives of toxicology · 2021Review
- Mutation of GGMP Repeat Segments ofInternational journal of molecular sciences · 2021Article
- Hsp70 Inhibits Aggregation of IAPP by Binding to the Heterogeneous Prenucleation Oligomers.Biophysical journal · 2021Article
- Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Heat shock proteins of 70 kDa (Hsp70s) are ubiquitous and highly conserved molecular chaperones. They play multiple essential roles in assisting with protein folding and maintaining protein homeostasis. Their chaperone activity has been proposed to require several rounds of binding to and release of polypeptide substrates at the substrate-binding domain (SBD) of Hsp70s. All available structures have revealed a single substrate-binding site in the SBD that binds a single segment of an extended polypeptide of 3-4 residues. However, this well-established single peptide-binding site alone has made it difficult to explain the efficient chaperone activity of Hsp70s. In this study, using purified proteins and site-directed mutagenesis, along with fluorescence polarization and luciferase-refolding assays, we report the unexpected discovery of a second peptide-binding site in Hsp70s. More importantly, the biochemical analyses suggested that this novel binding site, named here P2, is essential for Hsp70 chaperone activity. Furthermore, cross-linking and mutagenesis studies indicated that this second binding site is in the SBD adjacent to the first binding site. Taken together, our results suggest that these two essential binding sites of Hsp70s cooperate in protein folding.
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