Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants.

@article{Dick1998ContributionOP,
  title={Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants.},
  author={Tobias P Dick and Alexander Konrad Nussbaum and Martin Deeg and Wolfgang Heinemeyer and Michael Groll and Markus Schirle and Wieland Keilholz and Stefan Stevanovi{\'c} and Dieter H. Wolf and Robert Huber and Hans Georg Rammensee and Hansjoerg Schild},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 40},
  pages={25637-46}
}
Proteasomes generate peptides that can be presented by major histocompatibility complex (MHC) class I molecules in vertebrate cells. Using yeast 20 S proteasomes carrying different inactivated beta-subunits, we investigated the specificities and contributions of the different beta-subunits to the degradation of polypeptide substrates containing MHC class I ligands and addressed the question of additional proteolytically active sites apart from the active beta-subunits. We found a clear… CONTINUE READING
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