ArticleJournal of the American Chemical Society2014
Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli.Metallomics : integrated biometal science · 2025Review
- Hsp70 Inhibits the Replication of Fowl Adenovirus Serotype 4 by Suppressing Viral Hexon with the Assistance of DnaJC7.Journal of virology · 2022Article
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- The potential value of cuprotosis (copper-induced cell death) in the therapy of clear cell renal cell carcinoma.American journal of cancer research · 2022Article
- Comparative Characterization ofBiomolecules · 2020Article
- Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The role of chaperones in iron-sulfur cluster biogenesis.FEBS letters · 2018Review
- Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium.Scientific reports · 2018Article
- Genetic variation in N- and C-terminal regions of bovineJournal of genomics · 2018Article
- Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis.eLife · 2017Article
- A disulfide-bonded DnaK dimer is maintained in an ATP-bound state.Cell stress & chaperones · 2017Article
- Understanding the role of dynamics in the iron sulfur cluster molecular machine.Biochimica et biophysica acta. General subjects · 2017Article
- Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Structure (London, England : 1993) · 2016Review
- Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein-Protein Interaction.Molecular biology and evolution · 2016Article
- Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Biochimica et biophysica acta · 2015Review
- Deletion of the Proposed Iron Chaperones IscA/SufA Results in Accumulation of a Red Intermediate Cysteine Desulfurase IscS in Escherichia coli.The Journal of biological chemistry · 2015Article
- How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Journal of molecular biology · 2015Review
- Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi.Biotechnology research international · 2015Review
- The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.Biochemistry · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The structural mechanism by which Hsp70-type chaperones interact with Hsp40-type co-chaperones has been of great interest, yet still remains a matter of debate. Here, we used solution NMR spectroscopy to investigate the ATP-/ADP-dependent interactions between Escherichia coli HscA and HscB, the specialized Hsp70/Hsp40 molecular chaperones that mediate iron-sulfur cluster transfer. We observed that NMR signals assigned to amino acid residues in the J-domain and its "HPD" motif of HscB broadened severely upon the addition of ATP-bound HscA, but these signals were not similarly broadened by ADP-bound HscA or the isolated nucleotide binding domain of HscA complexed with either ATP or ADP. An HscB variant with an altered HPD motif, HscB(H32A,P33A,D34A), failed to manifest WT-like NMR signal perturbations and also abolished WT-like stimulation of ATP hydrolysis by HscA. In addition, residues 153-171 in the C-terminal region of HscB exhibited NMR signal perturbations upon interaction with HscA, alone or complexed with ADP or ATP. These results demonstrate that the HPD motif in the J-domain of HscB directly interacts with ATP-bound HscA and suggest that a second, less nucleotide-dependent binding site for HscA resides in the C-terminal region of HscB.
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