scholarly journals Stress response in yeast mRNA export factor: reversible changes in Rat8p localization are caused by ethanol stress but not heat shock

2004 ◽  
Vol 117 (18) ◽  
pp. 4189-4197 ◽  
Author(s):  
R. Takemura
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Mrna Export ◽  
Ethanol Stress

scholarly journals Association of Constitutive Hyperphosphorylation of Hsf1p with a Defective Ethanol Stress Response in Saccharomyces cerevisiae Sake Yeast Strains

2011 ◽  
Vol 78 (2) ◽  
pp. 385-392 ◽  
Author(s):  
Chiemi Noguchi ◽  
Daisuke Watanabe ◽  
Yan Zhou ◽  
Takeshi Akao ◽  
Hitoshi Shimoi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Stress Response ◽  
Heat Shock ◽  
Laboratory Strain ◽  
Underlying Mechanism ◽  
Ethanol Stress ◽  
Heat Shock Element ◽  
Content Type ◽  
Yeast Strains ◽  
Acute Ethanol

ABSTRACTModern sake yeast strains, which produce high concentrations of ethanol, are unexpectedly sensitive to environmental stress during sake brewing. To reveal the underlying mechanism, we investigated a well-characterized yeast stress response mediated by a heat shock element (HSE) and heat shock transcription factor Hsf1p inSaccharomyces cerevisiaesake yeast. The HSE-lacZactivity of sake yeast during sake fermentation and under acute ethanol stress was severely impaired compared to that of laboratory yeast. Moreover, the Hsf1p of modern sake yeast was highly and constitutively hyperphosphorylated, irrespective of the extracellular stress. SinceHSF1allele replacement did not significantly affect the HSE-mediated ethanol stress response or Hsf1p phosphorylation patterns in either sake or laboratory yeast, the regulatory machinery of Hsf1p is presumed to function differently between these types of yeast. To identify phosphatases whose loss affected the control of Hsf1p, we screened a series of phosphatase gene deletion mutants in a laboratory strain background. Among the 29 mutants, a Δppt1mutant exhibited constitutive hyperphosphorylation of Hsf1p, similarly to the modern sake yeast strains, which lack the entirePPT1gene locus. We confirmed that the expression of laboratory yeast-derived functionalPPT1recovered the HSE-mediated stress response of sake yeast. In addition, deletion ofPPT1in laboratory yeast resulted in enhanced fermentation ability. Taken together, these data demonstrate that hyperphosphorylation of Hsf1p caused by loss of thePPT1gene at least partly accounts for the defective stress response and high ethanol productivity of modern sake yeast strains.

Heat shock and ethanol stress provoke distinctly different responses in 3′-processing and nuclear export of HSP mRNA in Saccharomyces cerevisiae

2008 ◽  
Vol 414 (1) ◽  
pp. 111-119 ◽  
Author(s):  
Shingo Izawa ◽  
Takeomi Kita ◽  
Kayo Ikeda ◽  
Yoshiharu Inoue
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Transcriptional Activation ◽  
Nuclear Export ◽  
Mrna Export ◽  
Yeast Cells ◽  
Nuclear Accumulation ◽  
Ethanol Stress ◽  
Nuclear Retention ◽  
Eukaryotic Gene

Under conditions of heat shock at 42 °C, mRNAs of HSP (heat shock protein) genes are exported out of the nucleus, whereas bulk poly(A)+ (polyadenylated) mRNA shows a nuclear accumulation in Saccharomyces cerevisiae. Such a selective mRNA export seems an efficacious strategy of yeast cells to adapt rapidly to stress. Although ethanol stress (10%, v/v) as well as heat shock blocks the export of bulk poly(A)+ mRNA, the differences and/or similarity between heat shock and ethanol stress in the mechanisms of selective mRNA export still remain to be clarified. We found that ethanol stress induced transcriptional activation of a subset of yeast HSP genes; however, intriguingly, most such transcripts remained in the nucleus in a hyperadenylated state and, as a consequence, were not translated into HSPs. Elimination of ethanol resulted in a rapid shortening of the poly(A) tails of HSP mRNAs, loss of their nuclear retention, and the coincidental synthesis of the respective HSPs. Since HSP mRNAs are selectively exported from the nucleus in heat-shocked cells, yeast cells respond differently to ethanol stress and heat shock in the 3′-processing and transport of HSP mRNAs. Furthermore, these results also suggest that hyperadenylation and nuclear retention of mRNAs might be used as a means to control eukaryotic gene expression under stressed conditions.

scholarly journals Antisense Downregulation of ς32 as a Transient Metabolic Controller in Escherichia coli: Effects on Yield of Active Organophosphorus Hydrolase

2000 ◽  
Vol 66 (10) ◽  
pp. 4366-4371 ◽  
Author(s):  
Ranjan Srivastava ◽  
Hyung Joon Cha ◽  
Marvin S. Peterson ◽  
William E. Bentley
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Stress Response ◽  
Heat Shock ◽  
Total Yield ◽  
Fold Increase ◽  
Organophosphorus Hydrolase ◽  
Ethanol Stress ◽  
Antisense Mrna ◽  
Partial Degradation

ABSTRACT Plasmids containing an antisense fragment of the ς32gene were constructed and introduced into Escherichia colicells. Downregulation of the ς32-mediated stress response was evaluated under heat shock and ethanol stress and during the production of organophosphorus hydrolase (OPH). Northern blot analyses revealed that ς32 sense mRNA was virtually undetected in antisense-producing cultures from 5 to 20 min after antisense induction. However, lower-molecular-weight bands were found, presumably due to partial degradation of ς32 mRNA. While a >10-fold increase in ς32 protein level was found under ethanol stress in the control cultures, antisense producing cultures resulted in a <3-fold increase, indicating downregulation of ς32. Correspondingly, antisense synthesis resulted in a decreased level of a ς32 regulated chaperone (GroEL) for the first 2 h after induction relative to control cultures without ς32 antisense mRNA. The total yield of OPH in the presence of ς32 antisense was, on average, 62% of the yield without antisense. However, during ς32 antisense production, a sixfold-higher specific OPH activity was observed compared to non-antisense-producing cultures.

scholarly journals Rox3 and Rts1 Function in the Global Stress Response Pathway in Baker's Yeast

Genetics ◽  
1996 ◽  
Vol 142 (4) ◽  
pp. 1083-1093 ◽  
Author(s):  
Carlos C Evangelista ◽  
Ana M Rodriguez Torres ◽  
M Paullin Limbach ◽  
Richard S Zitomer
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Osmotic Stress ◽  
Regulatory Element ◽  
Regulatory Region ◽  
Mitogen Activated Protein Kinase ◽  
Regulatory Subunit ◽  
Temperature Sensitive ◽  
Global Stress ◽  
Rna Accumulation

Abstract Yeast respond to a variety of stresses through a global stress response that is mediated by a number of signal transduction pathways and the cis-acting STRE DNA sequence. The CYC7 gene, encoding iso-2-cytochrome c, has been demonstrated to respond to heat shock, glucose starvation, approach-to-stationary phase, and, as we demonstrate here, to osmotic stress. This response was delayed in a the hogl-Δ1 strain implicating the Hog1 mitogen-activated protein kinase cascade, a known component of the global stress response. Deletion analysis of the CYC7 regulatory region suggested that three STRE elements were each capable of inducing the stress response. Mutations in the ROX3 gene prevented CYC7 RNA accumulation during heat shock and osmotic stress. ROX3 RNA levels were shown to be induced by stress through a novel regulatory element. A selection for high-copy suppressors of a ROX3 temperature-sensitive allele resulted in the isolation of RTS1, encoding a protein with homology to the B′ regulatory subunit of protein phosphatase 2A0. Deletion of RTS1 caused temperature and osmotic sensitivity and increased accumulation of CYC7 RNA under all conditions. Over-expression of this gene caused increased CYC7 RNA accumulation in rox3 mutants but not in wild-type cells.

scholarly journals Genome-wide identification and analysis of the heat shock transcription factor family in moso bamboo (Phyllostachys edulis)

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Bin Huang ◽  
Zhinuo Huang ◽  
Ruifang Ma ◽  
Jialu Chen ◽  
Zhijun Zhang ◽  
...  
Keyword(s):  
Heat Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Gene Family ◽  
Regulatory Elements ◽  
Moso Bamboo ◽  
Naphthalene Acetic Acid ◽  
Plant Responses ◽  
Heat Stress Response ◽  
Regulatory Pathways

AbstractHeat shock transcription factors (HSFs) are central elements in the regulatory network that controls plant heat stress response. They are involved in multiple transcriptional regulatory pathways and play important roles in heat stress signaling and responses to a variety of other stresses. We identified 41 members of the HSF gene family in moso bamboo, which were distributed non-uniformly across its 19 chromosomes. Phylogenetic analysis showed that the moso bamboo HSF genes could be divided into three major subfamilies; HSFs from the same subfamily shared relatively conserved gene structures and sequences and encoded similar amino acids. All HSF genes contained HSF signature domains. Subcellular localization prediction indicated that about 80% of the HSF proteins were located in the nucleus, consistent with the results of GO enrichment analysis. A large number of stress response–associated cis-regulatory elements were identified in the HSF upstream promoter sequences. Synteny analysis indicated that the HSFs in the moso bamboo genome had greater collinearity with those of rice and maize than with those of Arabidopsis and pepper. Numerous segmental duplicates were found in the moso bamboo HSF gene family. Transcriptome data indicated that the expression of a number of PeHsfs differed in response to exogenous gibberellin (GA) and naphthalene acetic acid (NAA). A number of HSF genes were highly expressed in the panicles and in young shoots, suggesting that they may have functions in reproductive growth and the early development of rapidly-growing shoots. This study provides fundamental information on members of the bamboo HSF gene family and lays a foundation for further study of their biological functions in the regulation of plant responses to adversity.

scholarly journals TOR and RAS pathways regulate desiccation tolerance inSaccharomyces cerevisiae

2013 ◽  
Vol 24 (2) ◽  
pp. 115-128 ◽  
Author(s):  
Aaron Z. Welch ◽  
Patrick A. Gibney ◽  
David Botstein ◽  
Douglas E. Koshland
Keyword(s):  
Growth Rate ◽  
Stress Response ◽  
Heat Shock ◽  
Desiccation Tolerance ◽  
Ribosome Biogenesis ◽  
Inverse Correlation ◽  
Fold Increase ◽  
Nutrient Deprivation ◽  
Camp Pathway ◽  
Dividing Cells

Tolerance to desiccation in cultures of Saccharomyces cerevisiae is inducible; only one in a million cells from an exponential culture survive desiccation compared with one in five cells in stationary phase. Here we exploit the desiccation sensitivity of exponentially dividing cells to understand the stresses imposed by desiccation and their stress response pathways. We found that induction of desiccation tolerance is cell autonomous and that there is an inverse correlation between desiccation tolerance and growth rate in glucose-, ammonia-, or phosphate-limited continuous cultures. A transient heat shock induces a 5000–fold increase in desiccation tolerance, whereas hyper-ionic, -reductive, -oxidative, or -osmotic stress induced much less. Furthermore, we provide evidence that the Sch9p-regulated branch of the TOR and Ras-cAMP pathway inhibits desiccation tolerance by inhibiting the stress response transcription factors Gis1p, Msn2p, and Msn4p and by activating Sfp1p, a ribosome biogenesis transcription factor. Among 41 mutants defective in ribosome biogenesis, a subset defective in 60S showed a dramatic increase in desiccation tolerance independent of growth rate. We suggest that reduction of a specific intermediate in 60S biogenesis, resulting from conditions such as heat shock and nutrient deprivation, increases desiccation tolerance.

scholarly journals Impaired Temperature Stress Response of a Streptococcus thermophilus deoD Mutant

2003 ◽  
Vol 69 (2) ◽  
pp. 1287-1289 ◽  
Author(s):  
Mario Varcamonti ◽  
Maria R. Graziano ◽  
Romilde Pezzopane ◽  
Gino Naclerio ◽  
Slavica Arsenijevic ◽  
...  
Keyword(s):  
Growth Rate ◽  
Stress Response ◽  
Heat Shock ◽  
Temperature Stress ◽  
Streptococcus Thermophilus ◽  
Wild Type ◽  
Temperature Shock ◽  
Dual Response ◽  
Survival Capacity

ABSTRACT An insertional deoD mutant of Streptococcus thermophilus strain SFi39 had a reduced growth rate at 20°C and an enhanced survival capacity to heat shock compared to the wild type, indicating that the deoD product is involved in temperature shock adaptation. We report evidence that ppGpp is implicated in this dual response.

Identification of cis and trans components of a novel heat shock stress regulatory pathway in Saccharomyces cerevisiae

1993 ◽  
Vol 13 (1) ◽  
pp. 248-256
Author(s):  
N Kobayashi ◽  
K McEntee
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Stress Response ◽  
Heat Shock ◽  
Reporter Gene ◽  
Heat Shock Element ◽  
Cis Acting ◽  
Heat Shock Stress ◽  
Specific Complex ◽  
Cis And Trans ◽  
Shock Stress

The stress-responsive DDR2 gene (previously called DDRA2) of Saccharomyces cerevisiae is transcribed at elevated levels following stress caused by heat shock or DNA damage. Previously, we identified a 51-bp promoter fragment, oligo31/32, which conferred heat shock inducibility on the heterologous CYC1-lacZ reporter gene in S. cerevisiae (N. Kobayashi and K. McEntee, Proc. Natl. Acad. Sci. USA 87:6550-6554, 1990). Using a series of synthetic oligonucleotides, we have identified a pentanucleotide, CCCCT (C4T), as an essential component of this stress response sequence. This element is not a binding site for the well-characterized heat shock transcription factor which recognizes a distinct cis-acting heat shock element in the promoters of many heat shock genes. Here we demonstrate the ability of oligonucleotides containing the C4T sequence to confer heat shock inducibility on the reporter gene and show that the presence of two such elements produces more than additive effects on induction. Gel retardation experiments have been used to demonstrate specific complex formation between C4T-containing fragments and one or more yeast proteins. Formation of these complexes was not competed by fragments containing mutations in the C4T sequence nor by heat shock element-containing competitor DNAs. Fragments containing the C4T element bound to a single 140-kDa polypeptide, distinct from heat shock transcription factors in yeast crude extracts. These experiments identify key cis- and trans-acting components of a novel heat shock stress response pathway in S. cerevisiae.

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