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TitleIn situ characterization of mitochondrial Hsp60-Hsp10 chaperone complex under folding stress.
Journal, issue, pagesSci Adv, Vol. 11, Issue 43, Page eadw6064, Year 2025
Publish dateOct 24, 2025
AuthorsMingyu Jung / Minjung Kim / Su Jin Ham / Jongkyeong Chung / Soung-Hun Roh /
PubMed AbstractMitochondrial proteostasis is critical for maintaining mitochondrial function, and its disruption induces mitochondrial unfolded protein response, which up-regulates chaperones to alleviate protein- ...Mitochondrial proteostasis is critical for maintaining mitochondrial function, and its disruption induces mitochondrial unfolded protein response, which up-regulates chaperones to alleviate protein-folding stress. However, how these chaperones mitigate protein-folding stress remains unclear. Here, using correlated cryo-electron tomography, we show that folding stress triggers marked mitochondrial morphological changes, including the accumulation of amorphous protein aggregates and increased abundance and spatial clustering of the mitochondrial heat shock protein 60-heat shock protein 10 (mtHsp60-Hsp10) complex. Subtomogram analysis revealed the in situ architecture and conformational heterogeneity of mtHsp60-Hsp10 under stress, which retains its canonical double-ring structure while adopting distinct football, half-football, and bullet-like states. Notably, the mtHsp60-Hsp10 complex encapsulates unstructured substrates through conserved hydrophobic interactions. We further demonstrate that knockdown of the mtHsp60-Hsp10 complex exacerbates folding stress, as evidenced by elevated cellular stress responses and activation of mitophagy. Our study defines the in situ structural properties of the mtHsp60-Hsp10 complex and provides mechanistic insight into how it safeguards mitochondrial proteostasis under folding stress.
External linksSci Adv / PubMed:41124257 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution7.3 - 27.0 Å
Structure data

62702

9l8p

EMDB-62702: mthsp60-hsp10_consensus
PDB-9l8p: in situ structure of mtHsp60-Hsp10
Method: EM (subtomogram averaging) / Resolution: 7.3 Å

EMDB-62703: mthsp60-hsp10_without_symmetry
Method: EM (subtomogram averaging) / Resolution: 8.1 Å

EMDB-62704: mthsp60-hsp10_with_additional_interaction
Method: EM (subtomogram averaging) / Resolution: 9.8 Å

EMDB-62711: mthsp60-hsp10 with sparse substrate density
Method: EM (subtomogram averaging) / Resolution: 8.5 Å

EMDB-62713: mthsp60-hsp10 with bulky substrate density on single chamber
Method: EM (subtomogram averaging) / Resolution: 8.7 Å

EMDB-62714: mthsp60-hsp10 with bulky substrate density in both chamber
Method: EM (subtomogram averaging) / Resolution: 8.5 Å

EMDB-62747: mthsp60-hsp10 with U-shaped substrate density
Method: EM (subtomogram averaging) / Resolution: 9.3 Å

EMDB-65492: In situ structure of mtHsp60-Hsp10 bullet-like conformation
Method: EM (subtomogram averaging) / Resolution: 21.0 Å

EMDB-65493: in situ structure of mtHsp60-Hsp10 half-football conformation
Method: EM (subtomogram averaging) / Resolution: 27.0 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCHAPERONE / mtHsp60-Hsp10

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