Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC

Stable Identifier
R-NUL-391408
Type
Reaction [dissociation]
Species
Mus musculus
Compartment
cytosol
ReviewStatus
5/5
General
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PNG
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 | PPTX  | SBGN
Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC
Group II chaperonins enclose substrate proteins following substrate binding through the formation of a "built- in" lid over the central cavity. Upon ATP binding, lid formation is triggered by the transition state of ATP hydrolysis (Meyer, et al., 2003). In the case of CCT-mediated tubulin folding, one or more rounds of ATP hydrolysis are likely required before the association of non-exchangeable GTP with chaperonin-bound alpha tubulin.
Literature References
PubMed ID Title Journal Year
8096061 Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin

Cowan, NJ, Chow, RL, Gao, Y, Vainberg, IE

Mol Cell Biol 1993
Participants
Input
Output
Orthologous Events
Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC (Homo sapiens)
Authored
Cowan, NJ  (2009-01-21)
Reviewed
Cowan, NJ  (2009-01-21)
Created
Matthews, L  (2009-02-21)
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