Cold response in Saccharomyces cerevisiae: New functions for old mechanisms. FEMS Microbiol Rev

Department of Biotechnology, Instituto de Agroquímica y Tecnología de los Alimentos, Consejo Superior de Investigaciones Científicas, Burjassot, Valencia, Spain.
FEMS Microbiology Reviews (Impact Factor: 13.24). 05/2007; 31(3):327-41. DOI: 10.1111/j.1574-6976.2007.00066.x
Source: PubMed


The response of yeast cells to sudden temperature downshifts has received little attention compared with other stress conditions. Like other organisms, both prokaryotes and eukaryotes, in Saccharomyces cerevisiae a decrease in temperature induces the expression of many genes involved in transcription and translation, some of which display a cold-sensitivity phenotype. However, little is known about the role played by many cold-responsive genes, the sensing and regulatory mechanisms that control this response or the biochemical adaptations at or near 0 degrees C. This review focuses on the physiological significance of cold-shock responses, emphasizing the molecular mechanisms that generate and transmit cold signals. There is now enough experimental evidence to conclude that exposure to low temperature protects yeast cells against freeze injury through the cold-induced accumulation of trehalose, glycerol and heat-shock proteins. Recent results also show that changes in membrane fluidity are the primary signal triggering the cold-shock response. Notably, this signal is transduced and regulated through classical stress pathways and transcriptional factors, the high-osmolarity glycerol mitogen-activated protein kinase pathway and Msn2/4p. Alternative cold-stress generators and transducers will also be presented and discussed.

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Available from: Jaime Aguilera, Feb 13, 2015
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    • "Nevertheless, evidence suggests that yeast viability decreases with storage time at 4ºC (Kandror et al., 2004) and especially below 0ºC (Hernández-López et al., 2003;Rodriguez-Vargas et al., 2007). Freezing stress causes serious cell injury, mainly due to the formation of intracellular ice crystals, dehydration and oxidative stress during the thawing process (Aguilera et al., 2007). Despite of this, the cellular responses that protect yeast cells against loss of viability at very low temperature have received little attention. "
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    ABSTRACT: At near-freezing temperatures (0–4 °C), the growth of the yeast Saccharomyces cerevisiae stops or is severely limited, and viability decreases. Under these conditions, yeast cells trigger a biochemical response, in which trehalose and glycerol accumulate and protect them against severe cold and freeze injury. However, the mechanisms that allow yeast cells to sustain this response have been not clarified. The effects of severe cold on the proteome of S. cerevisiae have been not investigated and its importance in providing cell survival at near-freezing temperatures and upon freezing remains unknown. Here, we have compared the protein profile of two industrial baker's yeast strains at 30 °C and 4 °C. Overall, a total of 16 proteins involved in energy-metabolism, translation and redox homeostasis were identified as showing increased abundance at 4 °C. The predominant presence of glycolytic proteins among those upregulated at 4 °C, likely represents a mechanism to maintain a constant supply of ATP for the synthesis of glycerol and other protective molecules. Accumulation of these molecules is by far the most important component in enhancing viability of baker's yeast strains upon freezing. Overexpression of genes encoding certain proteins associated with translation or redox homeostasis provided specifically protection against extreme cold damage, underlying the importance of these functions in the near-freezing response.
    Full-text · Article · Jan 2016 · Journal of Biotechnology
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    • "These heat shock proteins are universally conserved across all organisms and have been very well characterized. However, the response to cold shock has been less well studied, although its effects on cellular physiology are known (Thieringer et al. 1998; Al-Fageeh and Smales 2006; Aguilera et al. 2007). Decreases in temperature cause a reduction in membrane fluidity, a reduction in enzymatic activity, the stabilization of DNA and RNA secondary structures, and the impairment of protein synthesis. "
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    ABSTRACT: We investigated the dynamics of a gene regulatory network controlling the cold shock response in budding yeast, Saccharomyces cerevisiae. The medium-scale network, derived from published genome-wide location data, consists of 21 transcription factors that regulate one another through 31 directed edges. The expression levels of the individual transcription factors were modeled using mass balance ordinary differential equations with a sigmoidal production function. Each equation includes a production rate, a degradation rate, weights that denote the magnitude and type of influence of the connected transcription factors (activation or repression), and a threshold of expression. The inverse problem of determining model parameters from observed data is our primary interest. We fit the differential equation model to published microarray data using a penalized nonlinear least squares approach. Model predictions fit the experimental data well, within the 95 % confidence interval. Tests of the model using randomized initial guesses and model-generated data also lend confidence to the fit. The results have revealed activation and repression relationships between the transcription factors. Sensitivity analysis indicates that the model is most sensitive to changes in the production rate parameters, weights, and thresholds of Yap1, Rox1, and Yap6, which form a densely connected core in the network. The modeling results newly suggest that Rap1, Fhl1, Msn4, Rph1, and Hsf1 play an important role in regulating the early response to cold shock in yeast. Our results demonstrate that estimation for a large number of parameters can be successfully performed for nonlinear dynamic gene regulatory networks using sparse, noisy microarray data. Electronic supplementary material The online version of this article (doi:10.1007/s11538-015-0092-6) contains supplementary material, which is available to authorized users.
    Full-text · Article · Sep 2015 · Bulletin of Mathematical Biology
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    • "It should also be recognized that cells respond to changes in growth temperature in ways other than by changes in membrane fatty acid composition, for example it is well documented that sterols influence membrane structure and function (Parks and Casey 1995; Daum et al. 1998; Sharma, 2006). Furthermore, the role of heat shock proteins, trehalose and glycerol in respect to yeast temperature adaptation, to both cold and heat, should also be taken into consideration (Tanghe et al. 2006; Aguilera et al. 2007). There have been very few published studies on temperature stress response in Antarctic yeasts and, although there have been some earlier reports on the synthesis of heat shock proteins in Antarctic yeasts (Deegenaars and Watson 1997, 1998) and in yeasts from the Arctic (Berg et al. 1987; Julseth and Inniss 1990), this is clearly an area that would provide valuable information in our understanding of mechanisms of temperature adaptation. "
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    ABSTRACT: The fatty acid profiles of Antarctic (n = 7) and non-Antarctic yeasts (n = 7) grown at different temperatures were analysed by gas chromatography-mass spectrometry. The Antarctic yeasts were enriched in oleic 18:1 (20-60 %), linoleic 18:2 (20-50 %) and linolenic 18:3 (5-40 %) acids with lesser amounts of palmitic 16:0 (<15 %) and palmitoleic 16:1 (<10 %) acids. The non-Antarctic yeasts (n = 4) were enriched in 18:1 (20-55 %, with R. mucilaginosa at 75-80 %) and 18:2 (10-40 %) with lesser amounts of 16:0 (<20 %), 16:1 (<20 %) and stearic 18:0 (<10 %) acids. By contrast, Saccharomyces cerevisiae strains (n = 3) were enriched in 16:1 (30-50 %) and 18:1 (20-40 %) with lesser amounts of 16:0 (10-25 %) and 18:0 (5-10 %) acids. Principal component analysis grouped the yeasts into three clusters, one belonging to the S. cerevisiae strains (enriched in 16:0, 16:1 and 18:1), one to the other non-Antarctic yeasts (enriched in 18:1 and 18:2) and the third to the Antarctic yeasts (enriched in 18:2 and 18:3).
    Full-text · Article · May 2014 · Antonie van Leeuwenhoek
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