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TitleMechanism of small heat shock protein client sequestration and induced polydispersity.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 3635, Year 2025
Publish dateApr 16, 2025
AuthorsAdam P Miller / Steve L Reichow /
PubMed AbstractSmall heat shock proteins (sHSPs) act as first responders during cellular stress, sequestering destabilized proteins (clients) to prevent aggregation and facilitate refolding or degradation. This ...Small heat shock proteins (sHSPs) act as first responders during cellular stress, sequestering destabilized proteins (clients) to prevent aggregation and facilitate refolding or degradation. This critical function, conserved across all life, is linked to proteostasis and protein misfolding diseases. However, the extreme molecular plasticity of sHSP/client complexes has limited mechanistic understanding. Here, we present high-resolution cryo-EM structures of Methanocaldococcus jannaschii sHSP (mjHSP16.5) in apo and multiple client-bound states. The ensemble reveals molecular mechanisms of client sequestration, highlighting cooperative chaperone-client interactions. Client engagement polarizes scaffold stability, promoting higher-order assembly and enhanced sequestration. Higher-order states suggest multiple sHSP/client assembly pathways, including subunit insertion at destabilized geometrical features. These findings provide critical insights into sHSP chaperone function and the interplay between polydispersity and client handling under stress.
External linksNat Commun / PubMed:40240363 / PubMed Central
MethodsEM (single particle)
Resolution2.35 - 4.71 Å
Structure data

49828

9nv4

EMDB-49828, PDB-9nv4:
mjHSP16.5 apo-contracted (37C)
Method: EM (single particle) / Resolution: 2.5 Å

49829

9nv7

EMDB-49829, PDB-9nv7:
mjHSP16.5 apo-expanded (37C)
Method: EM (single particle) / Resolution: 2.35 Å

49830

9nv8

EMDB-49830, PDB-9nv8:
mjHSP16.5 apo 75C
Method: EM (single particle) / Resolution: 2.86 Å

49832

9nvc

EMDB-49832, PDB-9nvc:
mjHSP16.5 24mer (+lysozyme, 75C)
Method: EM (single particle) / Resolution: 2.6 Å

49834

9nvf

EMDB-49834, PDB-9nvf:
mjHSP16.5 26mer (+lysozyme, 75C)
Method: EM (single particle) / Resolution: 3.65 Å

49836

9nvi

EMDB-49836, PDB-9nvi:
mjHSP16.5 32mer (+lysozyme, 75C)
Method: EM (single particle) / Resolution: 4.37 Å

49837

9nvj

EMDB-49837, PDB-9nvj:
mjHSP16.5 34mer (+lysozyme, 75C)
Method: EM (single particle) / Resolution: 4.71 Å

49838

9nvk

EMDB-49838, PDB-9nvk:
mjHSP16.5 36mer (+lysozyme, 75C)
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • methanocaldococcus jannaschii (archaea)
  • methanocaldococcus jannaschii dsm 2661 (archaea)
  • Escherichia coli BL21(DE3) (bacteria)
KeywordsCHAPERONE / sHSP / thermophilic / holdase / holds / thermophile

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