The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae

Matsumoto, Ryosuke; Akama, Kuniko; Rakwal, Randeep; Iwahashi, Hitoshi

doi:10.1186/1471-2164-6-141

Cited by 39 publications

(34 citation statements)

References 61 publications

(60 reference statements)

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“…The number of induced genes was larger than that of the repressed genes in most functional categories, especially in "Energy", "Protein activity of regulation" and "Cell rescue, defence and virulence". However, the number of repressed genes in category of "Protein synthesis" and "Transcription" was larger than that of the induced genes, in agreement with a previous expression profiling study of heat shock stress in wild S. cerevisiae (28).…”

Section: Meta-analysis and Identification Of Commonly Transient Heat supporting

confidence: 91%

A strategy for meta-analysis of short time series microarray datasets

Sun

Guo³

et al. 2009

Front Biosci

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Many time series microarray experiments have relatively short (less than ten) time points and lack in repeats, weakening the confidence of results. Combining the microarray data from different groups may improve the statistical power of detecting differentially expressed genes. However, few efforts have been taken to combine or compare the time-course array datasets generated by independent groups. Here we demonstrated a suitable strategy for meta-analysis of short time series microarray datasets and implemented this strategy on four published heat shock microarray datasets of Saccharomyces Cerevisiae. We first assessed the significance of each gene in each datasets based on area calculation and the null distribution of the areas. Then the similarity of significance values across datasets was assessed with meta-analysis methods, yielding a set of transient heat shock stress sensitive genes. Following correlation calculation helped us to combine the transformed data at the same time points of each gene. Further bioinformatic investigation showed the significance of our strategy, and also indicated some interesting features of regulatory systems in S. cerevisiae during transient heat stress.

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Section: Meta-analysis and Identification Of Commonly Transient Heat supporting

confidence: 91%

A strategy for meta-analysis of short time series microarray datasets

Sun

Guo³

et al. 2009

Front Biosci

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“…It seems possible that HSR becomes involved in alleviating stress in the secretory pathway under specific physiologic conditions. For instance, during heat stress, UPR is activated (Gasch et al , 2000; Matsumoto et al , 2005) together with HSR to ameliorate protein misfolding in the secretory pathway. Consistent with this idea, ire1 Δ cells are sensitive to heat stress (Supplementary Figure S3).…”

Section: Discussionmentioning

confidence: 99%

Heat shock response relieves ER stress

Liu

Chang

2008

EMBO J

149

126

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Accumulation of misfolded protein in the endoplasmic reticulum (ER) causes stress. The unfolded protein response (UPR), a transcriptional induction pathway, is activated to relieve ER stress. Although UPR is not essential for viability, UPR‐deficient cells are more sensitive to ER stress; ire1Δ cells cannot grow when challenged with tunicamycin or by overexpression of misfolded CPY*. In these cells, multiple functions are defective, including translocation, ER‐associated degradation (ERAD), and ER‐to‐Golgi transport. We tested whether heat shock response (HSR) can relieve ER stress. Using a constitutively active Hsf1 transcription factor to induce HSR without temperature shift, we find that HSR rescues growth of stressed ire1Δ cells, and partially relieves defects in translocation and ERAD. Cargo‐specific effects of constitutively active Hsf1 on ER‐to‐Golgi transport are correlated with enhanced protein levels of the respective cargo receptors. In vivo, HSR is activated by ER stress, albeit to a lower level than that caused by heat. Genomic analysis of HSR targets reveals that >25% have function in common with UPR targets. We propose that HSR can relieve stress in UPR‐deficient cells by affecting multiple ER activities.

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“…can lead to an imbalance between the protein folding load and the protein folding capacity in the ER lumen, resulting in an accumulation of malfolded proteins, i.e. ER stress [ 17 – 19 ]. In response to ER stress, eukaryotic cells have evolved signalling pathways that induce the unfolded protein response (UPR).…”

Section: Introductionmentioning

confidence: 99%

Investigation of protein secretion and secretion stress in Ashbya gossypii

et al. 2014

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BackgroundAshbya gossypii is a filamentous Saccharomycete used for the industrial production of riboflavin that has been recently explored as a host system for recombinant protein production. To gain insight into the protein secretory pathway of this biotechnologically relevant fungus, we undertook genome-wide analyses to explore its secretome and its transcriptional responses to protein secretion stress.ResultsA computational pipeline was used to predict the inventory of proteins putatively secreted by A. gossypii via the general secretory pathway. The proteins actually secreted by this fungus into the supernatants of submerged cultures in minimal and rich medium were mapped by two-dimensional gel electrophoresis, revealing that most of the A. gossypii secreted proteins have an isoelectric point between 4 and 6, and a molecular mass above 25 kDa. These analyses together indicated that 1-4% of A. gossypii proteins are likely to be secreted, of which less than 33% are putative hydrolases. Furthermore, transcriptomic analyses carried out in A. gossypii cells under recombinant protein secretion conditions and dithiothreitol-induced secretion stress unexpectedly revealed that a conventional unfolded protein response (UPR) was not activated in any of the conditions, as the expression levels of several well-known UPR target genes (e.g. IRE1, KAR2, HAC1 and PDI1 homologs) remained unaffected. However, several other genes involved in protein unfolding, endoplasmatic reticulum-associated degradation, proteolysis, vesicle trafficking, vacuolar protein sorting, secretion and mRNA degradation were up-regulated by dithiothreitol-induced secretion stress. Conversely, the transcription of several genes encoding secretory proteins, such as components of the glycosylation pathway, was severely repressed by dithiothreitolConclusionsThis study provides the first insights into the secretion stress response of A. gossypii, as well as a basic understanding of its protein secretion potential, which is more similar to that of yeast than to that of other filamentous fungi. Contrary to what has been widely described for yeast and fungi, a conventional UPR was not observed in A. gossypii, but alternative protein quality control mechanisms enabled it to cope with secretion stress. These data will help provide strategies for improving heterologous protein secretion in A. gossypii.Electronic supplementary materialThe online version of this article (doi:10.1186/1471-2164-15-1137) contains supplementary material, which is available to authorized users.

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The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae

Cited by 39 publications

References 61 publications

A strategy for meta-analysis of short time series microarray datasets

A strategy for meta-analysis of short time series microarray datasets

Heat shock response relieves ER stress

Investigation of protein secretion and secretion stress in Ashbya gossypii

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