ArticleMolecular bioSystems2012
Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome.
Article in Molecular bioSystems, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
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- Structural Features of a Tiny Viral Protein, ORF7b of SARS-CoV-2.International journal of molecular sciences · 2026Article
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- Tandem repeats of highly bioluminescent NanoLuc are refolded noncanonically by the Hsp70 machinery.Protein science : a publication of the Protein Society · 2024Article
- Gene cloning and characterization of a novel recombinant 40-kDa heat shock protein from Mesobacillus persicus B48.World journal of microbiology & biotechnology · 2023Article
- Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future.The journal of physical chemistry. B · 2022Article
- Multivalent protein-protein interactions are pivotal regulators of eukaryotic Hsp70 complexes.Cell stress & chaperones · 2022Review
- The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones.Frontiers in molecular biosciences · 2022Article
- Mechanical Stability of a Small, Highly-Luminescent Engineered Protein NanoLuc.International journal of molecular sciences · 2020Article
- Hsp70 and NF-kB Mediated Control of Innate Inflammatory Responses in a Canine Macrophage Cell Line.International journal of molecular sciences · 2020Article
- UbcH5 Interacts with Substrates to Participate in Lysine Selection with the E3 Ubiquitin Ligase CHIP.Biochemistry · 2020Article
- Heat Shock Protein DnaJ inMicroorganisms · 2020Article
- Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor.Nature communications · 2019Article
- mRNA Engineering for the Efficient Chaperone-Mediated Co-Translational Folding of Recombinant Proteins inInternational journal of molecular sciences · 2019Article
- 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
- Synergy of Sodium Nitroprusside and Nitrate in Inhibiting the Activity of Sulfate Reducing Bacteria in Oil-Containing Bioreactors.Frontiers in microbiology · 2018Article
- From Fuzzy to Function: The New Frontier of Protein-Protein Interactions.Accounts of chemical research · 2017Article
- Antimicrobial Effects of Free Nitrous Acid on Desulfovibrio vulgaris: Implications for Sulfide-Induced Corrosion of Concrete.Applied and environmental microbiology · 2016Article
- How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Journal of molecular biology · 2015Review
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
In Escherichia coli, the molecular chaperones DnaK and DnaJ cooperate to assist the folding of newly synthesized or unfolded polypeptides. DnaK and DnaJ bind to hydrophobic motifs in these proteins and they also bind to each other. Together, this system is thought to be sufficiently versatile to act on the entire proteome, which creates interesting challenges in understanding the interactions between DnaK, DnaJ and their thousands of potential substrates. To address this question, we computationally predicted the number and frequency of DnaK- and DnaJ-binding motifs in the E. coli proteome, guided by free energy-based binding consensus motifs. This analysis revealed that nearly every protein is predicted to contain multiple DnaK- and DnaJ-binding sites, with the DnaJ sites occurring approximately twice as often. Further, we found that an overwhelming majority of the DnaK sites partially or completely overlapped with the DnaJ-binding motifs. It is well known that high concentrations of DnaJ inhibit DnaK-DnaJ-mediated refolding. The observed overlapping binding sites suggest that this phenomenon may be explained by an important balance in the relative stoichiometry of DnaK and DnaJ. To test this idea, we measured the chaperone-assisted folding of two denatured substrates and found that the distribution of predicted DnaK- and DnaJ-binding sites was indeed a good predictor of the optimal stoichiometry required for folding. These studies provide insight into how DnaK and DnaJ might cooperate to maintain global protein homeostasis.
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