PXD045382

PXD045382 is an original dataset announced via ProteomeXchange.

Title	Sse1, Hsp110 chaperone of yeast, controls the cellular fate during Endoplasmic Reticulum-stress
Description	Sse1, yeast cytosolic Hsp110 chaperone, is a wellknown Nucleotide Exchange Factor (NEF), a protein-disaggregase and a Chaperone linked to Protein Synthesis (CLIPS). Here we demonstrate SSE1’s genetic interaction with IRE1 and HAC1, the Endoplasmic Reticulum-Unfolded Protein Response (ER-UPR) sensors. sse1Δ strain exhibits an ER-UPR signalling-dependent resistance to tunicamycin-induced ER stress. Importantly, ER-stress-responsive reorganization of translating ribosomes from polysomes to monosomes is inefficient in SSE1 deleted strain leading to uninterrupted protein translation and starkly different ER-UPR kinetics. sse1Δ exhibits faster ER-UPR induction and quicker reversal to basal state compared to wildtype (WT) cells. Interestingly, ER-stress mediated yeast cell division arrest is escaped in sse1Δ strain during long term tunicamycin stress indicating important role of this chaperone in controlling cell division during ER stress. Furthermore, sse1Δ strain shows significantly higher cell viability in comparison to WT yeast, following short-term as well as long-term tunicamycin stress. In summary, we show that cytosolic chaperone Sse1 genetically interacts with ER-UPR pathway, controls the kinetics of ER-UPR, stress-induced cell division arrest and cell viability during global ER stress by tunicamycin.
HostingRepository	PRIDE
AnnounceDate	2024-04-19
AnnouncementXML	Submission_2024-04-18_22:40:17.367.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Mainak Pratim Jha
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	iodoacetamide derivatized residue
Instrument	TripleTOF 6600

Revision	Datetime	Status	ChangeLog Entry
0	2023-09-14 04:05:31	ID requested
⏵ 1	2024-04-18 22:40:18	announced

10.1093/g3journal/jkae075;

Jha MP, Kumar V, Ghosh A, Mapa K, Sse1, Hsp110 chaperone of yeast, controls the cellular fate during endoplasmic reticulum stress. G3 (Bethesda), 14(6):(2024) [pubmed]

submitter keyword: cell cycle arrest, Heat Shock Protein 110, Endoplasmic Reticulum Unfolded Protein Response,Molecular Chaperone, Tunicamycin, Protein Homeostasis, Heat Shock Protein 70

Koyeli Mapa
contact affiliation	Protein Homeostasis Laboratory, Department of Life Sciences, School of Natural Sciences, Shiv Nadar Institution of Eminence, Delhi-NCR, Greater Noida, Gautam Buddha Nagar, Uttar Pradesh 201314, India.
contact email	koyeli.mapa@snu.edu.in
lab head
Mainak Pratim Jha
contact affiliation	PhD Scholar, Department of Life Sciences, School of Natural Sciences, Shiv Nadar Institution of Eminence (University)
contact email	mj216@snu.edu.in
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD045382
     1. Label: PRIDE project
     2. Name: Sse1, Hsp110 chaperone of yeast, controls the cellular fate during Endoplasmic Reticulum-stress