Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase.

@article{Nishikawa2004MassSA,
  title={Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase.},
  author={Hiroyuki Nishikawa and Seido Ooka and Ko Sato and Kei Arima and Joji Okamoto and Rachel E. Klevit and Mamoru Fukuda and Tomohiko Ohta},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 6},
  pages={3916-24}
}
The breast and ovarian cancer suppressor BRCA1 acquires significant ubiquitin ligase activity when bound to BARD1 as a RING heterodimer. Although the activity may well be important for the role of BRCA1 as a tumor suppressor, the biochemical consequence of the activity is not yet known. Here we report that BRCA1-BARD1 catalyzes Lys-6-linked polyubiquitin… CONTINUE READING