Abstract：
: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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Spiess C,Miller EJ,McClellan AJ,Frydman Jdoi
10.1016/j.molcel.2006.09.003subject
Has Abstractpub_date
2006-10-06 00:00:00pages
25-37issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(06)00631-9journal_volume
24pub_type
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