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The Ability of DNAJB6b to Suppress Amyloid Formation Depends on the Chaperone Aggregation State.
Carlsson, Andreas; Axell, Emil; Emanuelsson, Cecilia; Olsson, Ulf; Linse, Sara.
Afiliação
  • Carlsson A; Lund University, Biochemistry and Structural Biology, Lund, Naturvetarvägen 16, 223 62, Sweden.
  • Axell E; Lund University, Biochemistry and Structural Biology, Lund, Naturvetarvägen 16, 223 62, Sweden.
  • Emanuelsson C; Lund University, Biochemistry and Structural Biology, Lund, Naturvetarvägen 16, 223 62, Sweden.
  • Olsson U; Lund University, Physical Chemistry, Lund, Naturvetarvägen 16, 223 62, Sweden.
  • Linse S; Lund University, Biochemistry and Structural Biology, Lund, Naturvetarvägen 16, 223 62, Sweden.
ACS Chem Neurosci ; 15(9): 1732-1737, 2024 05 01.
Article em En | MEDLINE | ID: mdl-38640082
ABSTRACT
For many chaperones, a propensity to self-assemble correlates with function. The highly efficient amyloid suppressing chaperone DNAJB6b has been reported to oligomerize. A key question is whether the DNAJB6b self-assemblies or their subunits are active units in the suppression of amyloid formation. Here, we address this question using a nonmodified chaperone. We use the well-established aggregation kinetics of the amyloid ß 42 peptide (Aß42) as a readout of the amyloid suppression efficiency. The experimental setup relies on the slow dissociation of DNAJB6b assemblies upon dilution. We find that the dissociation of the chaperone assemblies correlates with its ability to suppress fibril formation. Thus, the data show that the subunits of DNAJB6b assemblies rather than the large oligomers are the active forms in amyloid suppression. Our results provide insights into how DNAJB6b operates as a chaperone and illustrate the importance of established assembly equilibria and dissociation rates for the design of kinetic experiments.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos beta-Amiloides / Chaperonas Moleculares / Proteínas de Choque Térmico HSP40 Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos beta-Amiloides / Chaperonas Moleculares / Proteínas de Choque Térmico HSP40 Idioma: En Ano de publicação: 2024 Tipo de documento: Article