Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes.

@article{Book2010AffinityPO,
  title={Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes.},
  author={Adam J Book and Nicholas P Gladman and Sang-Sook Lee and Mark A Scalf and Lloyd M. Smith and Richard D Vierstra},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 33},
  pages={25554-69}
}
Selective proteolysis in plants is largely mediated by the ubiquitin (Ub)/proteasome system in which substrates, marked by the covalent attachment of Ub, are degraded by the 26 S proteasome. The 26 S proteasome is composed of two subparticles, the 20 S core protease (CP) that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the CP lumen for breakdown. Here, we describe an affinity method to rapidly purify… CONTINUE READING