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- Title
Sse1, Hsp110 chaperone of yeast, controls the cellular fate during endoplasmic reticulum stress.
- Authors
Jha, Mainak Pratim; Kumar, Vignesh; Ghosh, Asmita; Mapa, Koyeli
- Abstract
Sse1 is a cytosolic Hsp110 molecular chaperone of yeast, Saccharomyces cerevisiae. Its multifaceted roles in cellular protein homeostasis as a nucleotide exchange factor (NEF), as a protein-disaggregase and as a chaperone linked to protein synthesis (CLIPS) are well documented. In the current study, we show that SSE1 genetically interacts with IRE1 and HAC1 , the endoplasmic reticulum-unfolded protein response (ER-UPR) sensors implicating its role in ER protein homeostasis. Interestingly, the absence of this chaperone imparts unusual resistance to tunicamycin-induced ER stress which depends on the intact Ire1 - Hac1 mediated ER-UPR signaling. Furthermore, cells lacking SSE1 show inefficient ER-stress-responsive reorganization of translating ribosomes from polysomes to monosomes that drive uninterrupted protein translation during tunicamycin stress. In consequence, the sse1 Δ strain shows prominently faster reversal from ER-UPR activated state indicating quicker restoration of homeostasis, in comparison to the wild-type (WT) cells. Importantly, Sse1 plays a critical role in controlling the ER-stress-mediated cell division arrest, which is escaped in sse1 Δ strain during chronic tunicamycin stress. Accordingly, sse1 Δ strain shows significantly higher cell viability in comparison to WT yeast imparting the stark fitness following short-term as well as long-term tunicamycin stress. These data, all together, suggest that cytosolic chaperone Sse1 is an important modulator of ER stress response in yeast and it controls stress-induced cell division arrest and cell death during overwhelming ER stress induced by tunicamycin.
- Subjects
ENDOPLASMIC reticulum; RIBOSOMES; NUCLEOTIDE exchange factors; GENETIC translation; MOLECULAR chaperones; YEAST; HEAT shock proteins; CELL division
- Publication
G3: Genes | Genomes | Genetics, 2024, Vol 14, Issue 6, p1
- ISSN
2160-1836
- Publication type
Article
- DOI
10.1093/g3journal/jkae075