Formation of proteasome-PA700 complexes directly correlates with activation of peptidase activity.

@article{Adams1998FormationOP,
  title={Formation of proteasome-PA700 complexes directly correlates with activation of peptidase activity.},
  author={George M. Adams and B Crotchett and Clive A. Slaughter and George N Demartino and Edward P. Gogol},
  journal={Biochemistry},
  year={1998},
  volume={37 37},
  pages={12927-32}
}
The proteolytic activity of the eukaryotic 20S proteasome is stimulated by a multisubunit activator, PA700, which forms both 1:1 and 2:1 complexes with the proteasome. Formation of the complexes is enhanced by an additional protein assembly called modulator, which also stimulates the enzymatic activity of the proteasome only in the presence of PA700. Here we show that the binding of PA700 to the proteasome is cooperative, as is the activation of the proteasome's intrinsic peptidase activity… CONTINUE READING

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