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Chaperonin CCT is required for the correct folding of eIF3h and eIF3i subunits.
Both CCT4 and CCT5 homo-oligomers have the property of forming 8-fold double rings absent the other subunits, and these complexes carry out chaperonin reactions without other partner subunits.
The chaperonin containing TCP1 (MIM 186980) complex (CCT), also called the TCP1 ring complex, consists of 2 back-to-back rings, each containing 8 unique but homologous subunits, such as CCT4. CCT assists the folding of newly translated polypeptide substrates through multiple rounds of ATP-driven release and rebinding of partially folded intermediate forms. Substrates of CCT include the cytoskeletal proteins actin (see MIM 102560) and tubulin (see MIM 191130), as well as alpha-transducin (MIM 139330) (Won et al., 1998
T-complex protein 1 subunit delta
, T-complex protein 1 delta subunit
, chaperonin containing TCP1, subunit 4 (delta)
, T-complex protein 1 subunit delta-like
, chaperonin containing t-complex polypeptide 1, delta subunit
, stimulator of TAR RNA-binding
, T complex protein 1, delta
, TCP-1 delta
, chaperonin subunit 4 (delta)