Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes.

@article{Hirano2006CooperationOM,
  title={Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes.},
  author={Yuko Mandai Hirano and Hidemi Hayashi and Shun-ichiro Iemura and Klavs B. Hendil and Shin-ichiro Niwa and Toshihiko Kishimoto and Masanori Kasahara and Tohru Natsume and Keiji Tanaka and Shigeo Murata},
  journal={Molecular cell},
  year={2006},
  volume={24 6},
  pages={977-84}
}
The 20S proteasome is a catalytic core of the 26S proteasome, a central enzyme in the degradation of ubiquitin-conjugated proteins. It is composed of 14 distinct gene products that form four stacked rings of seven subunits each, alpha(1-7)beta(1-7)beta(1-7)alpha(1-7). It is reported that the biogenesis of mammalian 20S proteasomes is assisted by proteasome-specific chaperones, named PAC1, PAC2, and hUmp1, but the details are still unknown. Here, we report the identification of a chaperone… CONTINUE READING

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