Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK).

The Journal of biological chemistry - 9 Jul 2010

Chang Lyra, Thompson Andrea D, Ung Peter, Carlson Heather A, Gestwicki Jason E

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphatases
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HSP70 Heat-Shock Proteins

Share to Molecular Chaperones

Share to Mutagenesis

Share to Protein Denaturation

Share to Protein Folding

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 20439464
DOI: 10.1074/jbc.M110.124149
PMCID: PMC2898401

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK).PMID 20439464Read ↗

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.Semantic proximity Read ↗

Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.Semantic proximity Read ↗

Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling.Semantic proximity Read ↗

Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding.Semantic proximity Read ↗

Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis.Semantic proximity Read ↗

Multistep mechanism of substrate binding determines chaperone activity of Hsp70.Semantic proximity Read ↗

Isolation and characterization of an Escherichia coli DnaK mutant with impaired ATPase activity.Semantic proximity Read ↗

Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.Semantic proximity Read ↗

Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK.Semantic proximity Read ↗

Conformational equilibria in allosteric control of Hsp70 chaperones.Semantic proximity Read ↗

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.Semantic proximity Read ↗

Directed evolution of the DnaK chaperone: mutations in the lid domain result in enhanced chaperone activity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.