Abstract
We describe the complete β-tubulin folding pathway. Folding intermediates produced via ATP–dependent interaction with cytosolic chaperonin undergo a sequence of interactions with four proteins (cofactors A, D, E, and C). The postchaperonin steps in the reaction cascade do not depend on ATP or GTP hydrolysis, although GTP plays a structural role in tubulin folding. Cofactors A and D function by capturing and stabilizing β-tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D–β-tubulin complex; interaction with cofactor C then causes the release of β-tubulin polypeptides that are committed to the native state. Sequence analysis identifies yeast homologs of cofactors D (cin1) and E (pac2), characterized by mutations that affect microtubule function.
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