ArticleProceedings of the National Academy of Sciences of the United States of America1998
Role of the J-domain in the cooperation of Hsp40 with Hsp70.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
130 citing papers in PubMed, 278 citations in OpenAlex.
- Phylogenomic and comparative analyses on protein sequences fromInternational journal of systematic and evolutionary microbiology · 2025Article
- Structural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12.Nature communications · 2025Article
- Neuronal Ceroid Lipofuscinosis-Concepts, Classification, and Avenues for Therapy.CNS neuroscience & therapeutics · 2025Review
- The J Domain Proteins ofInternational journal of molecular sciences · 2024Review
- Review
- Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Review
- Gene cloning and characterization of a novel recombinant 40-kDa heat shock protein from Mesobacillus persicus B48.World journal of microbiology & biotechnology · 2023Article
- Large-scale identification of genes involved in septal pore plugging in multicellular fungi.Nature communications · 2023Article
- Article
- Leveraging the Structure of DNAJA1 to Discover Novel Potential Pancreatic Cancer Therapies.Biomolecules · 2022Article
- Multivalent protein-protein interactions are pivotal regulators of eukaryotic Hsp70 complexes.Cell stress & chaperones · 2022Review
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- DnaJC7 in Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2022Review
- A J-Protein OsDjC46 Interacts with ZFP36 to Participate in ABA-Mediated Antioxidant Defense in Rice.Antioxidants (Basel, Switzerland) · 2022Article
- Insights from a vertebrate model organism on the molecular mechanisms of whole-body dehydration tolerance.Molecular and cellular biochemistry · 2021Review
- The unfolded protein response plays dual roles in rice stripe virus infection through fine-tuning the movement protein accumulation.PLoS pathogens · 2021Article
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Hsp40 proteins phase separate to chaperone the assembly and maintenance of membraneless organelles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance.Molecular and cellular biology · 2020Article
- The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020Review
70 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at intermediate stages of folding, assembly, and translocation across membranes. Binding of protein substrates to the DnaK C-terminal domain is controlled by ATP binding and hydrolysis in the N-terminal ATPase domain. The interaction of DnaJ with DnaK is mediated at least in part by the highly conserved N-terminal J-domain of DnaJ that includes residues 2-75. Heteronuclear NMR experiments with uniformly 15N-enriched DnaJ2-75 indicate that the chemical environment of residues located in helix II and the flanking loops is perturbed on interaction with DnaK or a truncated DnaK molecule, DnaK2-388. NMR signals corresponding to these residues broaden and exhibit changes in chemical shifts in the presence of DnaK(MgADP). Addition of MgATP largely reversed the broadening, indicating that NMR signals of DnaJ2-75 respond to ATP-dependent changes in DnaK. The J-domain interaction is localized to the ATPase domain of DnaK and is likely to be dominated by electrostatic interactions. The results suggest that the J-domain tethers DnaK to DnaJ-bound substrates, which DnaK then binds with its C-terminal peptide-binding domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.