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Structure. 2012 May 9;20(5):814-25. doi: 10.1016/j.str.2012.03.007. Epub 2012 Apr 12.

The molecular architecture of the eukaryotic chaperonin TRiC/CCT.

Author information

1
Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland.

Abstract

TRiC/CCT is a highly conserved and essential chaperonin that uses ATP cycling to facilitate folding of approximately 10% of the eukaryotic proteome. This 1 MDa hetero-oligomeric complex consists of two stacked rings of eight paralogous subunits each. Previously proposed TRiC models differ substantially in their subunit arrangements and ring register. Here, we integrate chemical crosslinking, mass spectrometry, and combinatorial modeling to reveal the definitive subunit arrangement of TRiC. In vivo disulfide mapping provided additional validation for the crosslinking-derived arrangement as the definitive TRiC topology. This subunit arrangement allowed the refinement of a structural model using existing X-ray diffraction data. The structure described here explains all available crosslink experiments, provides a rationale for previously unexplained structural features, and reveals a surprising asymmetry of charges within the chaperonin folding chamber.

PMID:
22503819
PMCID:
PMC3350567
DOI:
10.1016/j.str.2012.03.007
[Indexed for MEDLINE]
Free PMC Article

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