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TitleThe Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis.
Journal, issue, pagesCell, Vol. 177, Issue 3, Page 751-765.e15, Year 2019
Publish dateApr 18, 2019
AuthorsDaniel Gestaut / Soung Hun Roh / Boxue Ma / Grigore Pintilie / Lukasz A Joachimiak / Alexander Leitner / Thomas Walzthoeni / Ruedi Aebersold / Wah Chiu / Judith Frydman /
PubMed AbstractMaintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the ...Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microscopy (cryo-EM), crosslinking-mass-spectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD. We find these hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates. The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis.
External linksCell / PubMed:30955883 / PubMed Central
MethodsEM (single particle)
Resolution6.5 - 8.7 Å
Structure data

0490

6nr8

EMDB-0490, PDB-6nr8:
hTRiC-hPFD Class6
Method: EM (single particle) / Resolution: 7.8 Å

0491

6nr9

EMDB-0491, PDB-6nr9:
hTRiC-hPFD Class5
Method: EM (single particle) / Resolution: 8.5 Å

0492

6nra

EMDB-0492, PDB-6nra:
hTRiC-hPFD Class1 (No PFD)
Method: EM (single particle) / Resolution: 7.7 Å

0493

6nrb

EMDB-0493, PDB-6nrb:
hTRiC-hPFD Class2
Method: EM (single particle) / Resolution: 8.7 Å

0494

6nrc

EMDB-0494, PDB-6nrc:
hTRiC-hPFD Class3
Method: EM (single particle) / Resolution: 8.3 Å

0495

6nrd

EMDB-0495, PDB-6nrd:
hTRiC-hPFD Class4
Method: EM (single particle) / Resolution: 8.2 Å

EMDB-0496:
hTRiC-hPFD all particles
Method: EM (single particle) / Resolution: 6.5 Å

Source
  • homo sapiens (human)
KeywordsCHAPERONE / TRiC/CCT / PFD / CryoEM / Molecular Chaperone / Protein folding

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