Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome

@article{BechOtschir2009PolyubiquitinSA,
  title={Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome},
  author={Dawadschargal Bech-Otschir and Annett Helfrich and Cordula Enenkel and Gesa Consiglieri and Michael Seeger and Hermann-Georg Holzh{\"u}tter and Burkhardt Dahlmann and Peter M Kloetzel},
  journal={Nature Structural &Molecular Biology},
  year={2009},
  volume={16},
  pages={219-225}
}
The 26S proteasome degrades polyubiquitylated (polyUb) proteins by an ATP-dependent mechanism. Here we show that binding of model polyUb substrates to the 19S regulator of mammalian and yeast 26S proteasomes enhances the peptidase activities of the 20S proteasome about two-fold in a process requiring ATP hydrolysis. Monoubiquitylated proteins or… CONTINUE READING