Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding.

@article{Grantham2000PartialOO,
  title={Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding.},
  author={Julie Grantham and Oscar Llorca and Jos{\'e} Mar{\'i}a Valpuesta and Keith Robert Willison},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 7},
  pages={4587-91}
}
The eukaryotic chaperonin containing T-complex polypeptide 1 (CCT) is required in vivo for the production of native actin and tubulin. It is a 900-kDa oligomer formed from two back-to-back rings, each containing eight different subunits surrounding a central cavity in which interactions with substrates are thought to occur. Here, we show that a monoclonal antibody recognizing the C terminus of the CCTalpha subunit can bind inside, and partially occlude, both cavities of apo-CCT. Rabbit… CONTINUE READING
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