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Effects of solution conditions on the self-assembly of the chaperone protein DNAJB6b

Carlsson, Andreas LU ; Maier, Victoria LU ; Fricke, Celia LU ; Pálmadóttir, Tinna LU ; André, Ingemar LU orcid ; Olsson, Ulf LU orcid and Linse, Sara LU (2025) In Communications Chemistry 8(1).
Abstract

Chaperone proteins are essential for maintaining proteostasis. Their main role is to assist with the folding of other proteins and to prevent the aggregation of misfolded proteins. The molecular chaperone DNAJB6b efficiently suppresses amyloid formation of several peptides. This activity may rely on the same physicochemical properties as those driving chaperone self-assembly into large micellar-like oligomers. We have therefore undertaken a systematic study of DNAJB6b’s self-assembly under different solution conditions. Using complementary biophysical techniques, we probe variations in aggregation number distribution and hydrodynamic radius, upon variation of pH, temperature, ionic strength, or anions across the Hofmeister series. We... (More)

Chaperone proteins are essential for maintaining proteostasis. Their main role is to assist with the folding of other proteins and to prevent the aggregation of misfolded proteins. The molecular chaperone DNAJB6b efficiently suppresses amyloid formation of several peptides. This activity may rely on the same physicochemical properties as those driving chaperone self-assembly into large micellar-like oligomers. We have therefore undertaken a systematic study of DNAJB6b’s self-assembly under different solution conditions. Using complementary biophysical techniques, we probe variations in aggregation number distribution and hydrodynamic radius, upon variation of pH, temperature, ionic strength, or anions across the Hofmeister series. We find that DNAJB6b maintains its propensity to self-assemble under all solution conditions examined. The size and compactness of the micelles change upon unfolding of the C-terminal domain, although a folded C-terminal domain does not drive micelle formation, which can likely be ascribed to hydrophobic interactions in the linker region. Mass photometry reveals that monomers of DNAJB6b coexist at equilibrium with the micelles. Furthermore, the free energy barrier for micelle dissociation into monomers was estimated by measuring dissociation rate constants at different temperatures. (Figure presented.)

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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Communications Chemistry
volume
8
issue
1
article number
289
publisher
Springer Nature
external identifiers
  • pmid:41034559
  • scopus:105017597317
ISSN
2399-3669
DOI
10.1038/s42004-025-01697-7
language
English
LU publication?
yes
id
1a113823-3b15-4821-a2a8-cbe7ee1a7e82
date added to LUP
2025-11-21 14:19:17
date last changed
2025-11-22 03:00:03
@article{1a113823-3b15-4821-a2a8-cbe7ee1a7e82,
  abstract     = {{<p>Chaperone proteins are essential for maintaining proteostasis. Their main role is to assist with the folding of other proteins and to prevent the aggregation of misfolded proteins. The molecular chaperone DNAJB6b efficiently suppresses amyloid formation of several peptides. This activity may rely on the same physicochemical properties as those driving chaperone self-assembly into large micellar-like oligomers. We have therefore undertaken a systematic study of DNAJB6b’s self-assembly under different solution conditions. Using complementary biophysical techniques, we probe variations in aggregation number distribution and hydrodynamic radius, upon variation of pH, temperature, ionic strength, or anions across the Hofmeister series. We find that DNAJB6b maintains its propensity to self-assemble under all solution conditions examined. The size and compactness of the micelles change upon unfolding of the C-terminal domain, although a folded C-terminal domain does not drive micelle formation, which can likely be ascribed to hydrophobic interactions in the linker region. Mass photometry reveals that monomers of DNAJB6b coexist at equilibrium with the micelles. Furthermore, the free energy barrier for micelle dissociation into monomers was estimated by measuring dissociation rate constants at different temperatures. (Figure presented.)</p>}},
  author       = {{Carlsson, Andreas and Maier, Victoria and Fricke, Celia and Pálmadóttir, Tinna and André, Ingemar and Olsson, Ulf and Linse, Sara}},
  issn         = {{2399-3669}},
  language     = {{eng}},
  number       = {{1}},
  publisher    = {{Springer Nature}},
  series       = {{Communications Chemistry}},
  title        = {{Effects of solution conditions on the self-assembly of the chaperone protein DNAJB6b}},
  url          = {{http://dx.doi.org/10.1038/s42004-025-01697-7}},
  doi          = {{10.1038/s42004-025-01697-7}},
  volume       = {{8}},
  year         = {{2025}},
}