ArticleProceedings of the National Academy of Sciences of the United States of America2011
Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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Who cites it
82 citing papers in PubMed.
- A low-complexity linker as a driver of intra- and intermolecular interactions in DNAJB chaperones.Nature communications · 2025Article
- Design principles to tailor Hsp104 therapeutics.Cell reports · 2024Article
- Pseudophosphorylation of single residues of the J-domain of DNAJA2 regulates the holding/folding balance of the Hsc70 system.Protein science : a publication of the Protein Society · 2024Article
- Design principles to tailor Hsp104 therapeutics.bioRxiv : the preprint server for biology · 2024Article
- J-domain Proteins form Binary Complexes with Hsp90 and Ternary Complexes with Hsp90 and Hsp70.Journal of molecular biology · 2023Article
- J-domain protein chaperone circuits in proteostasis and disease.Trends in cell biology · 2023Review
- Identification and functional analysis of novel protein-encoding sequences related to stress-resistance.Frontiers in microbiology · 2023Article
- RNA-sequencing Reveals Differentially Expressed Genes of Laying Hens Fed Baihu Decoction Under Heat Shock.The journal of poultry science · 2023Article
- Heat-Induced Proteotoxic Stress Response in Placenta-Derived Stem Cells (PDSCs) Is Mediated through HSPA1A and HSPA1B with a Potential Higher Role for HSPA1B.Current issues in molecular biology · 2022Article
- Mutagenesis and structural modeling implicate RME-8 IWN domains as conformational control points.PLoS genetics · 2022Article
- Neutron crystallographic analysis of the nucleotide-binding domain of Hsp72 in complex with ADP.IUCrJ · 2022Article
- Multivalent protein-protein interactions are pivotal regulators of eukaryotic Hsp70 complexes.Cell stress & chaperones · 2022Review
- Hidden information on protein function in censuses of proteome foldedness.Nature communications · 2022Article
- Abrogating the Interaction Between p53 and Mortalin (Grp75/HSPA9/mtHsp70) for Cancer Therapy: The Story so far.Frontiers in cell and developmental biology · 2022Review
- Comparative Proteomic Analysis of Psychrophilic vs. Mesophilic Bacterial Species Reveals Different Strategies to Achieve Temperature Adaptation.Frontiers in microbiology · 2022Article
- Identification and expression analysis of heat-shock proteins in wheat infected with powdery mildew and stripe rust.The plant genome · 2021Article
- Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership.Cell stress & chaperones · 2021Article
- Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone.Nature communications · 2021Article
- The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021Review
- The J- and G/F-domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance.FEBS open bio · 2020Article
22 more citing papers are in PubMed but not listed here.
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Abstract
The heat shock protein 70 kDa (Hsp70)/DnaJ/nucleotide exchange factor system assists in intracellular protein (re)folding. Using solution NMR, we obtained a three-dimensional structure for a 75-kDa Hsp70-DnaJ complex in the ADP state, loaded with substrate peptide. We establish that the J domain (residues 1-70) binds with its positively charged helix II to a negatively charged loop in the Hsp70 nucleotide-binding domain. The complex shows an unusual "tethered" binding mode which is stoichiometric and saturable, but which has a dynamic interface. The complex represents part of a triple complex of Hsp70 and DnaJ both bound to substrate protein. Mutagenesis data indicate that the interface is also of relevance for the interaction of Hsp70 and DnaJ in the ATP state. The solution complex is completely different from a crystal structure of a disulfide-linked complex of homologous proteins [Jiang, et al. (2007) Mol Cell 28:422-433].
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