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- W4376640517 abstract "Arsenite causes proteotoxicity by targeting nascent proteins for misfolding and aggregation. Here, we assessed how selected yeast chaperones and ubiquitin ligases contribute to proteostasis during arsenite stress. Loss of the ribosome‐associated chaperones Zuo1, Ssz1, and Ssb1/Ssb2 reduced global translation and protein aggregation, and increased arsenite resistance. Loss of cytosolic GimC/prefoldin function led to defective aggregate clearance and arsenite sensitivity. Arsenite did not induce ribosomal stalling or impair ribosome quality control, and ribosome‐associated ubiquitin ligases contributed little to proteostasis. Instead, the cytosolic ubiquitin ligase Rsp5 was important for aggregate clearance and resistance. Our study suggests that damage prevention, by decreased aggregate formation, and damage elimination, by enhanced aggregate clearance, are important protective mechanisms that maintain proteostasis during arsenite stress." @default.
- W4376640517 created "2023-05-17" @default.
- W4376640517 creator A5046632831 @default.
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- W4376640517 creator A5067142271 @default.
- W4376640517 creator A5067922621 @default.
- W4376640517 creator A5068258493 @default.
- W4376640517 date "2023-05-24" @default.
- W4376640517 modified "2023-10-14" @default.
- W4376640517 title "Yeast chaperones and ubiquitin ligases contribute to proteostasis during arsenite stress by preventing or clearing protein aggregates" @default.
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- W4376640517 doi "https://doi.org/10.1002/1873-3468.14638" @default.
- W4376640517 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37191881" @default.
- W4376640517 hasPublicationYear "2023" @default.
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