Journal
MOLECULAR CELL
Volume 24, Issue 1, Pages 25-37Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2006.09.003
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Funding
- NCI NIH HHS [CA 09302] Funding Source: Medline
- NIGMS NIH HHS [R01 GM074074-02, R21 GM 75166, R01 GM074074-01, R21 GM075166, R01 GM074074-04, R01 GM074074-03, R01 GM074074, R01 GM074074-01S1, GM 74074] Funding Source: Medline
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The ring-shaped hetero-oligomeric chaperonin TRiC/CCT uses ATP to fold a diverse subset of eukaryotic proteins. To define the basis of TRiC/CCT substrate recognition, we mapped the chaperonin interactions with the VHL tumor suppressor. VHL has two well-defined TRiC binding determinants. Each determinant contacts a specific subset of chaperonin subunits, indicating that TRiC paralogs exhibit distinct but overlapping specificities. The substrate binding site in these subunits localizes to a helical region in the apical domains that is structurally equivalent to that of bacterial chaperonins. Transferring the distal portion of helix 11 between TRiC subunits suffices to transfer specificity for a given substrate motif. We conclude that the architecture of the substrate binding domain is evolutionarily conserved among eukaryotic and bacterial chaperonins. The unique combination of specificity and plasticity in TRiC substrate binding may diversify the range of motifs recognized by this chaperonin and contribute to its unique ability to fold eukaryotic proteins.
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