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TitleStructural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 11, Year 2021
Publish dateMar 16, 2021
AuthorsJonathan J Knowlton / Daniel Gestaut / Boxue Ma / Gwen Taylor / Alpay Burak Seven / Alexander Leitner / Gregory J Wilson / Sreejesh Shanker / Nathan A Yates / B V Venkataram Prasad / Ruedi Aebersold / Wah Chiu / Judith Frydman / Terence S Dermody /
PubMed AbstractIntracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also ...Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1) facilitates folding of a subset of proteins with folding constraints such as complex topologies. To better understand the mechanism of TRiC folding, we investigated the biogenesis of an obligate TRiC substrate, the reovirus σ3 capsid protein. We discovered that the σ3 protein interacts with a network of chaperones, including TRiC and prefoldin. Using a combination of cryoelectron microscopy, cross-linking mass spectrometry, and biochemical approaches, we establish functions for TRiC and prefoldin in folding σ3 and promoting its assembly into higher-order oligomers. These studies illuminate the molecular dynamics of σ3 folding and establish a biological function for TRiC in virus assembly. In addition, our findings provide structural and functional insight into the mechanism by which TRiC and prefoldin participate in the assembly of protein complexes.
External linksProc Natl Acad Sci U S A / PubMed:33836586 / PubMed Central
MethodsEM (single particle)
Resolution4.5 - 6.2 Å
Structure data

23522

7lum

EMDB-23522: TRiC-substrate complex in ATP/AlFx closed state
PDB-7lum: Human TRiC in ATP/AlFx closed state
Method: EM (single particle) / Resolution: 4.5 Å

23526

7lup

EMDB-23526, PDB-7lup:
Human TRiC/CCT complex with reovirus outer capsid protein sigma-3
Method: EM (single particle) / Resolution: 6.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • Mammalian orthoreovirus 3 Dearing
  • reovirus type 3 (strain dearing)
KeywordsCHAPERONE / tric / cct / reovirus capsid / sigma 3

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