20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals.

@article{Tallec200720SPA,
  title={20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals.},
  author={Beno{\^i}t Le Tallec and Marie-B{\'e}n{\'e}dicte Barrault and R{\'e}gis Courbeyrette and Rapha{\"e}l Gu{\'e}rois and Marie-Claude Marsolier-Kergoat and Anne Peyroche},
  journal={Molecular cell},
  year={2007},
  volume={27 4},
  pages={660-74}
}
The 20S proteasome is the catalytic core of the 26S proteasome, a central enzyme in the ubiquitin-proteasome system. Its assembly proceeds in a multistep and orderly fashion. Ump1 is the only well-described chaperone dedicated to the assembly of the 20S proteasome in yeast. Here, we report a phenotype related to the DNA damage response that allowed us to isolate four other chaperones of yeast 20S proteasomes, which we named Poc1-Poc4. Poc1/2 and Poc3/4 form two pairs working at different stages… CONTINUE READING
61 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 61 extracted citations

Similar Papers

Loading similar papers…