In vitro reconstitution of SCF substrate ubiquitination with purified proteins.

@article{Petroski2005InVR,
  title={In vitro reconstitution of SCF substrate ubiquitination with purified proteins.},
  author={Matthew D. Petroski and Raymond J Deshaies},
  journal={Methods in enzymology},
  year={2005},
  volume={398},
  pages={143-58}
}
The development of in vitro systems to monitor ubiquitin ligase activity with highly purified proteins has allowed for new insights into the mechanisms of protein ubiquitination to be uncovered. This chapter describes the methodologies employed to reconstitute ubiquitination of the budding yeast cyclin-dependent kinase inhibitor Sic1 by the evolutionarily conserved ubiquitin ligase SCF(Cdc4) and its ubiquitin-conjugating enzyme Cdc34. Based on our experience in reconstituting Sic1… CONTINUE READING

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