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TitleAsymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.
Journal, issue, pagesbioRxiv, Year 2023
Publish dateMay 15, 2023
AuthorsJulian R Braxton / Hao Shao / Eric Tse / Jason E Gestwicki / Daniel R Southworth /
PubMed AbstractThe mitochondrial chaperonin, mtHsp60, promotes the folding of newly imported and transiently misfolded proteins in the mitochondrial matrix, assisted by its co-chaperone mtHsp10. Despite its ...The mitochondrial chaperonin, mtHsp60, promotes the folding of newly imported and transiently misfolded proteins in the mitochondrial matrix, assisted by its co-chaperone mtHsp10. Despite its essential role in mitochondrial proteostasis, structural insights into how this chaperonin binds to clients and progresses through its ATP-dependent reaction cycle are not clear. Here, we determined cryo-electron microscopy (cryo-EM) structures of a hyperstable disease-associated mtHsp60 mutant, V72I, at three stages in this cycle. Unexpectedly, client density is identified in all states, revealing interactions with mtHsp60's apical domains and C-termini that coordinate client positioning in the folding chamber. We further identify a striking asymmetric arrangement of the apical domains in the ATP state, in which an alternating up/down configuration positions interaction surfaces for simultaneous recruitment of mtHsp10 and client retention. Client is then fully encapsulated in mtHsp60/mtHsp10, revealing prominent contacts at two discrete sites that potentially support maturation. These results identify a new role for the apical domains in coordinating client capture and progression through the cycle, and suggest a conserved mechanism of group I chaperonin function.
External linksbioRxiv / PubMed:37293102 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 3.8 Å
Structure data

29813

8g7j

EMDB-29813, PDB-8g7j:
mtHsp60 V72I apo
Method: EM (single particle) / Resolution: 3.4 Å

29814

8g7k

EMDB-29814, PDB-8g7k:
mtHsp60 V72I apo focus
Method: EM (single particle) / Resolution: 3.8 Å

29815

8g7l

EMDB-29815, PDB-8g7l:
ATP-bound mtHsp60 V72I
Method: EM (single particle) / Resolution: 2.5 Å

29816

8g7m

EMDB-29816, PDB-8g7m:
ATP-bound mtHsp60 V72I focus
Method: EM (single particle) / Resolution: 3.2 Å

29817

8g7n

EMDB-29817, PDB-8g7n:
ATP- and mtHsp10-bound mtHsp60 V72I
Method: EM (single particle) / Resolution: 2.7 Å

29818

8g7o

EMDB-29818, PDB-8g7o:
ATP- and mtHsp10-bound mtHsp60 V72I focus
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCHAPERONE / chaperonin / ATPase / foldase

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