The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

@article{Nocker1996TheMP,
  title={The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.},
  author={Steven Van Nocker and Seth E Sadis and David M. Rubin and Michael L. Glickman and Haiqing Fu and Olivier Coux and Inge M Wefes and Daniel Daniel Finley and Richard D Vierstra},
  journal={Molecular and cellular biology},
  year={1996},
  volume={16 11},
  pages={6020-8}
}
The 26S proteasome is an essential proteolytic complex that is responsible for degrading proteins conjugated with ubiquitin. It has been proposed that the recognition of substrates by the 26S proteasome is mediated by a multiubiquitin-chain-binding protein that has previously been characterized in both plants and animals. In this study, we identified a Saccharomyces cerevisiae homolog of this protein, designated Mcb1. Mcb1 copurified with the 26S proteasome in both conventional and nickel… CONTINUE READING

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