Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae.

@article{Ghislain1996Cdc48pIW,
  title={Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae.},
  author={Michel Ghislain and R. J{\"u}rgen Dohmen and Fr{\'e}d{\'e}ric L{\'e}vy and Alexander Varshavsky},
  journal={The EMBO journal},
  year={1996},
  volume={15 18},
  pages={4884-99}
}
A library of random 10 residue peptides fused to the N-terminus of a reporter protein was screened in the yeast Saccharomyces cerevisiae for sequences that can target the reporter for degradation by the N-end rule pathway, a ubiquitin (Ub)-dependent proteolytic system that recognizes potential substrates through binding to their destabilizing N-terminal residues. One of the N-terminal sequences identified by this screen was used in a second screen for mutants incapable of degrading the… CONTINUE READING
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