ArticleBMC genomics2005
The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae.
Article in BMC genomics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Article
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- Intracellular aggregation of the transthyretin protein is limited by Hsp70 chaperones.bioRxiv : the preprint server for biology · 2025Article
- Clearing the JUNQ: the molecular machinery for sequestration, localization, and degradation of the JUNQ compartment.Frontiers in molecular biosciences · 2024Article
- Transcription factors enhancing synthesis of recombinant proteins and resistance to stress in Yarrowia lipolytica.Applied microbiology and biotechnology · 2023Article
- BRANEnet: embedding multilayer networks for omics data integration.BMC bioinformatics · 2022Article
- "Fight-flight-or-freeze" - how Yarrowia lipolytica responds to stress at molecular level?Applied microbiology and biotechnology · 2022Review
- Epigenetic Response ofMicroorganisms · 2021Article
- HacA Governs Virulence Traits and Adaptive Stress Responses inFrontiers in microbiology · 2020Article
- Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s.Current genetics · 2019Review
- Mitochondrial protein-induced stress triggers a global adaptive transcriptional programme.Nature cell biology · 2019Article
- Filamentous fungi-like secretory pathway strayed in a yeast system: peculiarities of Yarrowia lipolytica secretory pathway underlying its extraordinary performance.Applied microbiology and biotechnology · 2019Review
- Investigation of protein secretion and secretion stress in Ashbya gossypii.BMC genomics · 2014Article
- Endoplasmic reticulum stress and fungal pathogenesis.Fungal biology reviews · 2014Article
- Garbage on, garbage off: new insights into plasma membrane protein quality control.Current opinion in cell biology · 2014Review
- Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activity.BMC genomics · 2014Article
- Polysome profiling reveals broad translatome remodeling during endoplasmic reticulum (ER) stress in the pathogenic fungus Aspergillus fumigatus.BMC genomics · 2014Article
- Saccharomyces cerevisiae genes involved in survival of heat shock.G3 (Bethesda, Md.) · 2013Article
- Effects of a defective endoplasmic reticulum-associated degradation pathway on the stress response, virulence, and antifungal drug susceptibility of the mold pathogen Aspergillus fumigatus.Eukaryotic cell · 2013Article
- Convergent evolution of heat-inducibility during subfunctionalization of the Hsp70 gene family.BMC evolutionary biology · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundA yeast strain lacking the two genes SSA1 and SSA2, which encode cytosolic molecular chaperones, acquires thermotolerance as well as the mild heat-shocked wild-type yeast strain. We investigated the genomic response at the level of mRNA expression to the deletion of SSA1/2 in comparison with the mild heat-shocked wild-type using cDNA microarray.
resultsYeast cDNA microarray analysis revealed that genes involved in the stress response, including molecular chaperones, were up-regulated in a similar manner in both the ssa1/2 deletion mutant and the mild heat-shocked wild-type. Genes involved in protein synthesis were up-regulated in the ssa1/2 deletion mutant, but were markedly suppressed in the mild heat-shocked wild-type. The genes involved in ubiquitin-proteasome protein degradation were also up-regulated in the ssa1/2 deletion mutant, whereas the unfolded protein response (UPR) genes were highly expressed in the mild heat-shocked wild-type. RT-PCR confirmed that the genes regulating protein synthesis and cytosolic protein degradation were up-regulated in the ssa1/2 deletion mutant. At the translational level, more ubiquitinated proteins and proteasomes were detected in the ssa1/2 deletion mutant, than in the wild-type, confirming that ubiquitin-proteasome protein degradation was up-regulated by the deletion of SSA1/2.
conclusionThese results suggest that the mechanism for rescue of denatured proteins in the ssa1/2 deletion mutant is different from that in the mild heat-shocked wild-type: Activated protein synthesis in the ssa1/2 deletion mutant supplies a deficiency of proteins by their degradation, whereas mild heat-shock induces UPR.
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