ArticleThe Journal of biological chemistry2010
Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK).
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 71 citations in OpenAlex.
- Hsp70 is phosphorylated in a conserved response to DNA damage and contributes to cell cycle control.eLife · 2026Article
- Article
- Mechanism of Hsp70 activation: How J-domain proteins push for ATP hydrolysis.PLoS computational biology · 2026Article
- A conserved Hsp70 phosphorylation regulates cell cycle progression after DNA damage.bioRxiv : the preprint server for biology · 2025Article
- DnaK duplication and specialization in bacteria correlates with increased proteome complexity.mSystems · 2024Article
- New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE.The Journal of biological chemistry · 2024Article
- J-domain protein chaperone circuits in proteostasis and disease.Trends in cell biology · 2023Review
- An allosteric inhibitor of bacterial Hsp70 chaperone potentiates antibiotics and mitigates resistance.Cell chemical biology · 2022Article
- RNA-Seq Transcriptomic Analysis of Green Tea Polyphenols Modulation of Differently Expressed Genes in Enterococcus faecalis Under Bile Salt Stress.Current microbiology · 2022Article
- Tryptophan scanning mutagenesis as a way to mimic the compound-bound state and probe the selectivity of allosteric inhibitors in cells.Chemical science · 2020Article
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- A Legionella pneumophila Kinase Phosphorylates the Hsp70 Chaperone Family to Inhibit Eukaryotic Protein Synthesis.Cell host & microbe · 2019Article
- Inhibitors and chemical probes for molecular chaperone networks.The Journal of biological chemistry · 2019Review
- A Local Allosteric Network in Heat Shock Protein 70 (Hsp70) Links Inhibitor Binding to Enzyme Activity and Distal Protein-Protein Interactions.ACS chemical biology · 2018Article
- High-throughput screen for inhibitors of protein-protein interactions in a reconstituted heat shock protein 70 (Hsp70) complex.The Journal of biological chemistry · 2018Article
- X-linked inhibitor of apoptosis protein (XIAP) is a client of heat shock protein 70 (Hsp70) and a biomarker of its inhibition.The Journal of biological chemistry · 2018Article
- Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions.The Journal of biological chemistry · 2017Article
- Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy.Cell chemical biology · 2016Article
- Protein Cross-Linking Capillary Electrophoresis for Protein-Protein Interaction Analysis.Analytical chemistry · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Escherichia coli 70-kDa heat shock protein, DnaK, is a molecular chaperone that engages in a variety of cellular activities, including the folding of proteins. During this process, DnaK binds its substrates in coordination with a catalytic ATPase cycle. Both the ATPase and protein folding activities of DnaK are stimulated by its co-chaperones, DnaJ and GrpE. However, it is not yet clear how changes in the stimulated ATPase rate of DnaK impact the folding process. In this study, we performed mutagenesis throughout the nucleotide-binding domain of DnaK to generate a collection of mutants in which the stimulated ATPase rates varied from 0.7 to 13.6 pmol/microg/min(-1). We found that this range was largely established by differences in the ability of the mutants to be stimulated by one or both of the co-chaperones. Next, we explored how changes in ATPase rate might impact refolding of denatured luciferase in vitro and found that the two activities were poorly correlated. Unexpectedly, we found several mutants that refold luciferase normally in the absence of significant ATP turnover, presumably by increasing the flexibility of DnaK. Finally, we tested whether DnaK mutants could complement growth of DeltadnaK E. coli cells under heat shock and found that the ability to refold luciferase was more predictive of in vivo activity than ATPase rate. This study provides insights into how flexibility and co-chaperone interactions affect DnaK-mediated ATP turnover and protein folding.
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