ArticleAngewandte Chemie (International ed. in English)2022
Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- DNAJB6: A guardian against neurodegeneration.Neural regeneration research · 2026Article
- Chaperone nanomotors with chemotactic ability for the treatment of Parkinson's disease.Science advances · 2025Article
- A low-complexity linker as a driver of intra- and intermolecular interactions in DNAJB chaperones.Nature communications · 2025Article
- Decoding chaperone complexes: Insights from NMR spectroscopy.Biophysics reviews · 2024Review
- Enzymatic and synthetic regulation of polypeptide folding.Chemical science · 2024Review
- The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation.BMC biology · 2023Article
- Distinguishing features of fold-switching proteins.Protein science : a publication of the Protein Society · 2023Review
- Chasing long-range evolutionary couplings in the AlphaFold era.Biopolymers · 2023Article
- Identification and Validation of a Novel Prognostic Signature Based on Ferroptosis-Related Genes in Ovarian Cancer.Vaccines · 2023Article
- Human J-Domain Protein DnaJB6 Protects Yeast from [Biology · 2022Article
- HDX-guided EPR spectroscopy to interrogate membrane protein dynamics.STAR protocols · 2022Article
- Review
- Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
DNAJB6 is a prime example of an anti-aggregation chaperone that functions as an oligomer. DNAJB6 oligomers are dynamic and subunit exchange is critical for inhibiting client protein aggregation. The T193A mutation in the C-terminal domain (CTD) of DNAJB6 reduces both chaperone self-oligomerization and anti-aggregation of client proteins, and has recently been linked to Parkinson's disease. Here, we show by NMR, including relaxation-based methods, that the T193A mutation has minimal effects on the structure of the β-stranded CTD but increases the population and rate of formation of a partially folded state. The results can be rationalized in terms of β-strand peptide plane flips that occur on a timescale of ≈100 μs and lead to global changes in the overall pleat/flatness of the CTD, thereby altering its ability to oligomerize. These findings help forge a link between chaperone dynamics, oligomerization and anti-aggregation activity which may possibly lead to new therapeutic avenues tuned to target specific substrates.
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