Trends in Microbiology
Volume 6, Issue 2, February 1998, Pages 43-44
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Differential role of Hsps and trehalose in stress tolerance

https://doi.org/10.1016/S0966-842X(97)01190-6Get rights and content

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    The exposure of cells to a mild HS increases survival upon a subsequent acute HS, likely as a result of increased expression of molecular chaperones and other protective factors (Chen et al., 2003; Richter et al., 2010; Vjestica et al., 2013). This is known as hormesis or thermo-tolerance (Parsell et al., 1993; Piper, 1996, 1998; Ribeiro et al., 1997). To test whether NuRs formation is prevented in conditions of thermo-tolerance, cells were exposed to 37°C for 45 min prior to the acute HS (Figure S3A).

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    In particular, it regulates neutral trehalase 1 (Nth1) activity [31,32], which is responsible for the rapid, nutrient-induced changes in trehalose content [33]. Trehalose disaccharide, comprising two glucose molecules, is accumulated by yeast to stabilize cellular components under stress conditions [34]. It is hydrolyzed by Nth1 upon recovery from stress [35].

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    However, the roles of the recycling of glycogen under some stress conditions have not yet been clarified. It has been reported that trehalose synthesis is stimulated by heat shock and osmotic stress (49-51) and that its accumulation correlates with thermotolerance of yeast cells (52-54). In our analysis, trehalose synthesis seemed to be stimulated by low temperature through cooperative regulation of a trehalose-synthesis multicomplex:PGM2 (phosphoglucomutase), UGP1 (UDP-glucose phrophosphorylase), TPS1 and TPS2(trehalose-6-phosphate synthases), and TSL1 (a 123-kDa regulatory subunit of trehalose-6-phosphate synthase-phosphatase complex) (Fig. 5, cluster 5D).

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