The molecular architecture of the eukaryotic chaperonin TRiC/CCT

Alexander Leitner, Lukasz A. Joachimiak, Andreas Bracher, Leonie Mönkemeyer, Thomas Walzthoeni, Bryan Chen, Sebastian Pechmann, Susan Holmes, Yao Cong, Boxue Ma, Steve Ludtke, Wah Chiu, F. Ulrich Hartl, Ruedi Aebersold, Judith Frydman

Research output: Contribution to journalArticlepeer-review

233 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)814-825
Number of pages12
Issue number5
StatePublished - May 9 2012
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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