Role of trehalose and heat in the structure of the C‐terminal activation domain of the heat shock transcription factor

Bulman, Amanda L.; Nelson, Hillary C. M.

doi:10.1002/prot.20371

Cited by 21 publications

(17 citation statements)

References 72 publications

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“…There is an example of the involvement of trehalose in the regulation of chaperone genes. In S. cerevisiae, it was suggested that trehalose is involved in the activity of heat-shock transcription factor (Bulman & Nelson, 2005), although the corresponding gene was not found in Anabaena PCC 7120. Whether the expression of alr2445 and all0641 is regulated directly or indirectly by trehalose in Anabaena PCC 7120 is a matter to be tested in future.…”

Section: Discussionmentioning

confidence: 99%

The role of a gene cluster for trehalose metabolism in dehydration tolerance of the filamentous cyanobacterium Anabaena sp. PCC 7120

et al. 2006

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Expression of the genes for trehalose synthesis (mts and mth, encoding maltooligosyl trehalose synthase and hydrolase) and trehalose hydrolysis (treH) in Anabaena sp. PCC 7120 was up-regulated markedly upon dehydration. However, the amount of trehalose accumulated during dehydration was small, whereas a large amount of sucrose was accumulated. Northern blotting analysis revealed that these genes were transcribed as an operon. Gene disruption of mth resulted in a decrease in the trehalose level and in tolerance during dehydration. In contrast, gene disruption of treH resulted in an increase in both the amount of trehalose and tolerance. These results suggest that trehalose is important for the dehydration tolerance of this cyanobacterium. The amount of trehalose accumulated during dehydration was small, corresponding to 0?05-0?1 % of dry weight, suggesting that trehalose did not stabilize proteins and membranes directly during dehydration. To reveal the role of trehalose, the expression profiles of the wild-type strain and gene disruptants during dehydration were compared by using oligomeric DNA microarray. It was found that the expression of two genes, one of which encodes a cofactor of a chaperone DnaK, correlated with trehalose content, suggesting that a chaperone system induced by trehalose is important for the dehydration tolerance of Anabaena sp. PCC 7120.

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Section: Discussionmentioning

confidence: 99%

The role of a gene cluster for trehalose metabolism in dehydration tolerance of the filamentous cyanobacterium Anabaena sp. PCC 7120

et al. 2006

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“…Trehalose may also confer a broader range of protection for proteins, as it was demonstrated to enhance the survival of yeast cells treated with hydrogen peroxide and to reduce the extent of protein carbonylation, a prime indicator of oxidative damage (21). Lastly, Nelson and colleagues reported the surprising finding that trehalose is required for maximal transcriptional activation by Hsf1, which may be tied to its observed ability to stabilize the tertiary structure of the carboxy-terminal activation domain (42,68). Altered cell wall and membrane dynamics.…”

Section: Physiological and Metabolic Adaptationmentioning

confidence: 99%

“…The CTA is predominantly unfolded under physiological conditions but exhibits a certain amount of secondary and tertiary structures, as measured by circular dichroism (CD) and protease resistance. The ␣-helical content can be significantly increased at high temperatures, at acidic pHs, or by the addition of the disaccharide trehalose, suggesting that the CTA undergoes distinct conformational changes under different conditions (42,336). Although both transactivation domains are strong constitutive activators when fused to a heterologous DNA-binding domain such as lexA, studies of a synthetic HSE-lacZ reporter suggested that the two transactivation domains respond differently to thermal stress (437).…”

Section: Hsf1mentioning

confidence: 99%

Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System

Verghese

Abrams

Wang

et al. 2012

Microbiol Mol Biol Rev

504

410

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SUMMARY The eukaryotic heat shock response is an ancient and highly conserved transcriptional program that results in the immediate synthesis of a battery of cytoprotective genes in the presence of thermal and other environmental stresses. Many of these genes encode molecular chaperones, powerful protein remodelers with the capacity to shield, fold, or unfold substrates in a context-dependent manner. The budding yeast Saccharomyces cerevisiae continues to be an invaluable model for driving the discovery of regulatory features of this fundamental stress response. In addition, budding yeast has been an outstanding model system to elucidate the cell biology of protein chaperones and their organization into functional networks. In this review, we evaluate our understanding of the multifaceted response to heat shock. In addition, the chaperone complement of the cytosol is compared to those of mitochondria and the endoplasmic reticulum, organelles with their own unique protein homeostasis milieus. Finally, we examine recent advances in the understanding of the roles of protein chaperones and the heat shock response in pathogenic fungi, which is being accelerated by the wealth of information gained for budding yeast.

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“…Both activation domains play important roles during the heat shock response, with each activation domain being critical for the expression of different subsets of HSPs (14). We have shown that trehalose increases both the secondary and tertiary structures of the CAD in vitro (8). To determine whether the CAD is required for the trehalose-dependent elevation in HSP mRNA levels, we deleted the CAD in our control and HT strains ( Table 1).…”

Section: Manipulation Of Trehalose Levels In Vivomentioning

confidence: 99%

“…We have previously shown that high concentrations of trehalose can increase the structure of the S. cerevisiae Hsf1 C-terminal activation domain in vitro, and this structural change is enhanced by temperature (8). We hypothesized that the effects of trehalose and elevated temperature on Hsf1's structure in vitro were linked to its dramatic increase in transcriptional activity after heat shock.…”

mentioning

confidence: 99%

The Natural Osmolyte Trehalose Is a Positive Regulator of the Heat-Induced Activity of Yeast Heat Shock Transcription Factor

Conlin

Nelson

2007

Molecular and Cellular Biology

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In Saccharomyces cerevisiae, the intracellular concentration of trehalose increases rapidly in response to many environmental stresses, including heat shock. These high trehalose levels have been correlated with tolerance to adverse conditions and led to the model that trehalose functions as a chemical cochaperone. Here, we show that the transcriptional activity of Hsf1 during the heat shock response depends on trehalose. Strains with low levels of trehalose have a diminished transcriptional response to heat shock, while strains with high levels of trehalose have an enhanced transcriptional response to heat shock. The enhanced transcriptional response does not require the other heat-responsive transcription factors Msn2/4 but is dependent upon heat and Hsf1. In addition, the phosphorylation levels of Hsf1 correlate with both transcriptional activity and the presence of trehalose. These in vivo results support a new role for trehalose, where trehalose directly modifies the dynamic range of Hsf1 activity and therefore influences heat shock protein mRNA levels in response to stress.Trehalose is a disaccharide of glucose that is found predominantly in bacteria, fungi (including yeasts), plants, and invertebrates. This natural osmolyte was initially characterized as a storage carbohydrate due to the high intracellular concentrations observed during these organisms' resting and anhydrobiotic states (reviewed in reference 55). Since these states involve the ability to survive stressful conditions, trehalose levels were then linked to thermotolerance, the ability of an organism to survive an otherwise lethal heat shock (reviewed in reference 47). Trehalose has been shown to stabilize the structures and enzymatic activities of proteins against thermal denaturation in vitro (15,27,63). In addition, trehalose can prevent the aggregation of misfolded proteins, including amyloidogenic proteins (3,11,27,33,46,52), and is being considered for clinical trials for Huntington's disease (53). Trehalose is more effective than other sugars in protecting proteins against thermal denaturation and aggregation because of its unusual ability to alter the water environment surrounding a protein, stabilizing the protein in its native conformation (1,30,34,48).In the yeast Saccharomyces cerevisiae, trehalose levels vary depending on the environment of the cell. The levels are almost undetectable during normal exponential growth. After heat shock, trehalose levels increase rapidly and dramatically, along with the accumulation of heat shock proteins (HSPs) (26,28). This rapid increase in trehalose has been attributed to the increase in both the translation of the genes involved in the synthesis of trehalose (TPS1 and TPS2) (4, 41, 58) and the substrates required for trehalose synthesis (1, 61). In addition, the enzymatic activity of TPS1 increases during the heat shock response (1, 38). High trehalose levels can stabilize enzymatic activity and can prevent the aggregation of exogenous proteins in vivo during heat shock (45,46). Trehalose is d...

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Role of trehalose and heat in the structure of the C‐terminal activation domain of the heat shock transcription factor

Cited by 21 publications

References 72 publications

The role of a gene cluster for trehalose metabolism in dehydration tolerance of the filamentous cyanobacterium Anabaena sp. PCC 7120

The role of a gene cluster for trehalose metabolism in dehydration tolerance of the filamentous cyanobacterium Anabaena sp. PCC 7120

Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System

The Natural Osmolyte Trehalose Is a Positive Regulator of the Heat-Induced Activity of Yeast Heat Shock Transcription Factor

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