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

The Role of the DIF Motif of the DnaJ (Hsp40) Co-chaperone in the Regulation of the DnaK (Hsp70) Chaperone Cycle

14 Mar 2006

Abstract excerpt

To perform effectively as a molecular chaperone, DnaK (Hsp70) necessitates the assistance of its DnaJ (Hsp40) co-chaperone partner, which efficiently stimulates its intrinsically weak ATPase activity and facilitates its interaction with polypeptide substrates. In this study, we address the function of the conserved glycine- and phenylalanine-rich (G/F-rich) region of the Escherichia coli DnaJ in the DnaK...

Read the complete abstract on PubMed

Topics

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

Share to Heat shock proteins research
Share to Protein Structure and Dynamics
Share to Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 16533811
DOI: 10.1074/jbc.m511192200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Role of the DIF Motif of the DnaJ (Hsp40) Co-chaperone in the Regulation of the DnaK (Hsp70) Chaperone CyclePMID 16533811Read ↗

Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.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 ↗

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

Mutation of GGMP Repeat Segments of Plasmodium falciparum Hsp70-1 Compromises Chaperone Function and Hop Co-Chaperone Binding.Semantic proximity Read ↗

Cytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK.Semantic proximity Read ↗

The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation.Semantic proximity Read ↗

Comparative characterisation of <i>Plasmodium falciparum</i> Hsp70-1 relative to <i>E. coli</i> DnaK reveals functional specificity of the parasite chaperoneSemantic proximity Read ↗

The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.Semantic proximity Read ↗

The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.Semantic proximity Read ↗

The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the <i>Escherichia coli</i> DnaJ molecular chaperoneSemantic proximity Read ↗

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

The Role of Non-Canonical Hsp70s (Hsp110/Grp170) in CancerSemantic proximity Read ↗

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