Abstract
Protein misfolding is a universal threat to cells. The ubiquitin-proteasome system mediates a cellular stress response capable of eliminating misfolded proteins. Here we identify Cuz1/Ynl155w as a component of the ubiquitin system, capable of interacting with both the proteasome and Cdc48. Cuz1/Ynl155w is regulated by the transcription factor Rpn4, and is required for cells to survive exposure to the trivalent metalloids arsenic and antimony. A related protein, Yor052c, shows similar phenotypes, suggesting a multicomponent stress response pathway. Cuz1/Ynl155w functions as a zinc-dependent ubiquitin-binding protein. Thus, Cuz1/Ynl155w is proposed to protect cells from metalloid-induced proteotoxicity by delivering ubiquitinated substrates to Cdc48 and the proteasome for destruction.
Highlights
Protein misfolding, a universal threat to cells, is dealt with by the ubiquitin-proteasome system
Two of the peptides were derived from the RP2CP species (Fig. 1A), and two from the regulatory particle (RP) species
Ynl155w Mediates a Novel Stress Response—All cells are exposed to environmental stresses, and the ability to respond to these insults is critical for survival
Summary
A universal threat to cells, is dealt with by the ubiquitin-proteasome system. Results: Ynl155w is a zinc-dependent ubiquitin-binding protein, interacts with proteasome and Cdc, and is essential for surviving metalloids. Conclusion: Ynl155w may protect cells from metalloid-induced proteotoxicity by delivering ubiquitinated proteins to Cdc and proteasome. Cuz1/ Ynl155w is regulated by the transcription factor Rpn, and is required for cells to survive exposure to the trivalent metalloids arsenic and antimony. Cuz1/Ynl155w is proposed to protect cells from metalloid-induced proteotoxicity by delivering ubiquitinated substrates to Cdc and the proteasome for destruction. We describe here a new component of the ubiquitin system, Ynl155w, a zinc finger protein capable of directly interacting with the proteasome and Cdc. Ynl155w functions as a zinc-dependent ubiquitin-binding protein, suggesting the hypothesis that Ynl155w protects cells from metalloid toxicity by delivering ubiquitinated proteins to Cdc and the proteasome for destruction
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
