Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.

ABSTRACT: Misfolded proteins are usually refolded to their functional conformations or degraded by quality control mechanisms. When misfolded proteins evade quality control, they can be sequestered to specific sites within cells to prevent the potential dysfunction and toxicity that arises from protein aggregation. Btn2 and Hsp42 are compartment-specific sequestrases that play key roles in the assembly of these deposition sites. Their exact intracellular functions and substrates are not well defined, particularly since heat stress sensitivity is not observed in deletion mutants. We show here that Btn2 and Hsp42 are required for tolerance to oxidative stress conditions induced by exposure to hydrogen peroxide. Btn2 and Hsp42 act to sequester oxidized proteins into defined PQC sites following ROS expo

SUBMITTER: Carter Z 

PROVIDER: S-EPMC10931478 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature