ArticleCell stress & chaperones2015
C-terminal amino acids are essential for human heat shock protein 70 dimerization.
Article in Cell stress & chaperones, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- A Proteogenomic Approach for the Identification of Virulence Factors in Leishmania Parasites.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Comparison of E. coli based self-inducible expression systems containing different human heat shock proteins.Scientific reports · 2021Article
- Comparative Characterization ofBiomolecules · 2020Article
- Review
- Oligomerization of Hsp70: Current Perspectives on Regulation and Function.Frontiers in molecular biosciences · 2019Review
- A self-inducible heterologous protein expression system in Escherichia coli.Scientific reports · 2016Article
- Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Structure (London, England : 1993) · 2016Review
- Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones.PLoS computational biology · 2015Article
- Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity.PloS one · 2015Article
- Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein.PloS one · 2015Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human inducible heat shock protein 70 (hHsp70), which is involved in several major pathologies, including neurodegenerative disorders and cancer, is a key molecular chaperone and contributes to the proper protein folding and maintenance of a large number of protein structures. Despite its role in disease, the current structural knowledge of hHsp70 is almost exclusively based on its Escherichia coli homolog, DnaK, even though these two proteins only share ~50 % amino acid identity. For the first time, we describe a complete heterologous production and purification strategy that allowed us to obtain a large amount of soluble, full-length, and non-tagged hHsp70. The protein displayed both an ATPase and a refolding activity when combined to the human Hsp40. Multi-angle light scattering and bio-layer interferometry analyses demonstrated the ability of hHsp70 to homodimerize. The role of the C-terminal part of hHsp70 was identified and confirmed by a study of a truncated version of hHsp70 that could neither dimerize nor present refolding activity.
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