Saccharomyces cerevisiae
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ABSTRACT:
PROVIDER: PRJNA147891 | ENA |
REPOSITORIES: ENA
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Project description:Yeast DNA microarray was used to assess and compare the global expression profile of strains harboring different family members of the major cytosolic Hsp70 family. Viability of a yeast strain deleted for all genes encoding members of the Hsp70-Ssa family (Ssa1/2/3/4) was maintained by the presence of a single Ssa family member expressed ectopically from a plasmid vector. The Hsp70-Ssa family constitutes the main source of Hsp70 molecular chaperone activity in the yeast cell. A yeast cell must actively express a member of this family to remain viable. Hsp70-Ssa are highly conserved both within yeast and amongst other species. Ssa1 and 2 are 97% identical at amino acid level and 80% identical to Ssa3 and 4. The aim of this study was to attribute specific functions to single Ssa family members by identifying specific genes or gene families whose expression was altered in the presence (or absence) of Ssa family members. Eight independent RNA samples were pooled to represent a single biological sample for expression analysis. For example, the single sample analyzed for cells harboring only Ssa1 is a pooled sample of eight independent RNA extractions. Hybridization was performed for cells harboring either Ssa1, Ssa2, Ssa3 or Ssa4 as the sole cytosolic Hsp70-Ssa family member. Gene expression profiles of Ssa2/3/4 were all compared to Ssa1.
2012-12-31 | E-GEOD-32433 | biostudies-arrayexpress
Project description:Yeast DNA microarray was used to assess and compare the global expression profile of strains harboring different family members of the major cytosolic Hsp70 family. Viability of a yeast strain deleted for all genes encoding members of the Hsp70-Ssa family (Ssa1/2/3/4) was maintained by the presence of a single Ssa family member expressed ectopically from a plasmid vector. The Hsp70-Ssa family constitutes the main source of Hsp70 molecular chaperone activity in the yeast cell. A yeast cell must actively express a member of this family to remain viable. Hsp70-Ssa are highly conserved both within yeast and amongst other species. Ssa1 and 2 are 97% identical at amino acid level and 80% identical to Ssa3 and 4. The aim of this study was to attribute specific functions to single Ssa family members by identifying specific genes or gene families whose expression was altered in the presence (or absence) of Ssa family members.
2012-12-31 | GSE32433 | GEO
Project description:Metabolic engineering strategies have been successfully implemented to improve the production of isobutanol, a next-generation biofuel, in Saccharomyces cerevisiae. Here, we explore how two of these strategies, pathway re-localization and redox cofactor-balancing, affect the performance and physiology of isobutanol producing strains. We equipped yeast with isobutanol cassettes which had either a mitochondrial or cytosolic localized isobutanol pathway and used either a redox-imbalanced (NADPH-dependent) or redox-balanced (NADH-dependent) ketoacid reductoisomerase enzyme. We then conducted transcriptomic, proteomic and metabolomic analyses to elucidate molecular differences between the engineered strains. Pathway localization had a large effect on isobutanol production with the strain expressing the mitochondrial localized enzymes producing 3.8-fold more isobutanol than strains expressing the cytosolic enzymes. Cofactor-balancing did not improve isobutanol titers and instead the strain with the redox-imbalanced pathway produced 1.5-fold more isobutanol than the balanced version, albeit at low overall pathway flux. Functional genomic analyses indicated that the poor performances of the cytosolic pathway strains were in part due to a shortage in cytosolic Fe-S clusters, which are required cofactors for the dihydroxyacid dehydratase enzyme. We then demonstrated that this cofactor limitation may be partially recovered by disrupting iron homeostasis with a fra2 mutation, thereby increasing cellular iron levels. The resulting isobutanol titer of the fra2-null strain harboring a cytosolic localized isobutanol pathway outperformed the strain with the mitochondrial localized pathway by 1.3-fold, demonstrating that both localizations can support flux to isobutanol.
2021-10-22 | GSE186126 | GEO
Project description:Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast
| PRJNA312727 | ENA
Project description:Yeast must respond rapidly to heat stress by activating multiple signaling pathways that preserve proteostasis. This includes induction of Hsf1 and Msn2/4-mediated transcription, cell integrity signaling, stress-triggered phase separation of proteins and inhibition of translation. How these pathways are so rapidly activated and co-ordinated remains unclear. We show that the mechanosensor Mid2 senses heat-induced membrane stretch and leads to rapid phosphorylation of the cytosolic Hsp70 Ssa1 at a well-conserved threonine (T492). Phosphorylation of T492 leads to epichaperome rearrangement which includes altered interaction with Hsf1, multiple ribosomal subunits, the Bck1 MEK, and Edc3. Taken together these results provide a comprehensive, unified theory of the global yeast shock response that is mediated by the Hsp70 chaperone code.
2024-11-21 | MSV000096492 | MassIVE
Project description:A systems approach to delineate functions of YAP family members
| PRJNA108695 | ENA
Project description:HSC70 is the cytosolic isoform of plant HSP70. We have found that HSC70 family proteins bind to the heat shock transcription factor A1s (HsfA1s), which are the master regulators of the heat shock response in plants, and supress their activity. To investigate the role of HSC70s in the regulation of HsfA1s and heat shock responses, we evaluated the effect of triple knock out of HSC70s on the transcriptome under the normal growth condition.
2021-12-01 | E-MTAB-8721 | biostudies-arrayexpress
Project description:We demonstrate that inhibition of HSP70 with MAL3-101 induces activation of the unfolded protein response, and that cells with acquired resistance upregulate a cytosolic HSP70 at the level of mRNA.
2016-05-15 | GSE80525 | GEO
Project description:In our global differential gene expression analyses,ETRAMP14.1, an ETRAMP family member was found to be highly transcribed in vivo in severe Malaria patients from highly endemic Indian region. This study for the first time reports the interaction of ETRAMP14.1 with PfEMP1, EXP2 and Hsp70-1. Therefore, we propose that ETRAMP14.1 facilitate PfEMP1 to cross the PVM via transcolon machinery component EXP2.
2015-08-28 | GSE72447 | GEO