Transcriptional activation mediated by the yeast AP-1 protein is required for normal cadmium tolerance.

Wemmie, John A.; Wu, Ai-Ling; Harshman, Keith; Parker, Carl S.; Moye‐Rowley, W. Scott

doi:10.1016/s0021-9258(17)36680-2

Cited by 84 publications

(13 citation statements)

References 33 publications

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“…The major H 2 O 2 response pathway in Saccharomyces cerevisiae involves the transcription factor Yap1 and the oxidant receptor protein Orp1 ( , ). This pathway is regulated by a novel disulfide bond-relay cascade to control the expression of ∼70 genes in response to H 2 O 2 ( , ).…”

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confidence: 99%

A Genetically Encoded Probe for Cysteine Sulfenic Acid Protein Modification in Vivo

Takanishi

Wood

2007

Biochemistry

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All organisms have defense mechanisms to combat the deleterious effects of oxidative damage produced by reactive oxidative species (ROS). Although it is known that ROS play a major role in oxidative damage, increasing evidence reveals that ROS have wider cellular effects through their role in many signal transduction pathways. Here we have adapted a redox-regulated domain from the Yap1 transcription factor in Saccharomyces cerevisiae to function as a general trap for proteins that form cysteine sulfenic acid (Cys-SOH) in vivo. In response to H2O2, the Yap1 probe forms mixed disulfide bonds with a variety of proteins. The formation of these protein complexes is time dependent and peroxide concentration dependent. Disulfide-bonded complex formation can be attenuated by the addition of dimedone, a compound that specifically reacts with Cys-SOH, indicating the specificity of the probe toward Cys-SOH. An efficient one-step purification procedure was developed for proteins trapped by the Yap1 probe, and the constituents were identified by mass spectrometry. This methodology identified six proteins in Escherichia coli that contain redox-active cysteine residues known to form Cys-SOH as part of their catalytic cycle. The results suggest that the Yap1 probe is useful for identifying Cys-SOH-regulated proteins and can be employed in any genetically tractable organism to monitor transient Cys-SOH formation in vivo.

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confidence: 99%

A Genetically Encoded Probe for Cysteine Sulfenic Acid Protein Modification in Vivo

Takanishi

Wood

2007

Biochemistry

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“…yAP-1 shows sequence homology to other bZIP transcription factors, and the isolated DNA-binding region from yAP-1 shows the induction of an R helix upon binding to its DNA recognition site, consistent with the leucine zipper motif (28). Functionally, yAP-1 regulates pleiotropic drug resistance and has been shown to be nonessential for cell viability under normal circumstances (29). yAP-1 has a strong affinity for the site 5′-AATTAGT-CAGCA-3′, known as the activator recognition element (ARE).…”

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confidence: 83%

Site-Specific Inhibition of Transcription Factor Binding to DNA by a Metallointercalator

1999

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The metallointercalator Lambda-1-Rh(MGP)2phi5+ binds tightly and specifically to the site 5'-CATATG-3' in the major groove of double helical DNA by a combination of direct readout and shape selection. To examine competitive interactions between this small metal complex and a DNA-binding transcription factor, the preferred binding site for Lambda-1-Rh(MGP)2phi5+ was engineered into the AP-1 recognition element (ARE) of the major-groove binding bZIP transcription factor yAP-1, the yeast analogue of mammalian AP-1. Binding experiments confirmed that the modified ARE retained normal yAP-1 binding affinity. Photocleavage experiments demonstrated that the modified ARE contained a high-affinity binding site for Lambda-1-Rh(MGP)2phi5+, whereas the native ARE showed no interaction. Competition experiments using gel shift mobility assays demonstrated that Lambda-1-Rh(MGP)2phi5+ at 120 nM competes 50% of yAP-1 binding to the 5'-CATATG-3' containing oligonucleotide. In contrast, competitive disruption of protein binding to the native ARE requires 3 microM Lambda-1-Rh(MGP)2phi5+. Metallointercalator derivatives, including geometric isomers of Lambda-1-Rh(MGP)2phi5+, show no specific binding to the target site and show no inhibition of yAP-1/DNA complexes at concentrations as high as 20 microM. Thus, metallointercalators can be tuned to show selectivity for major groove sites on DNA comparable to transcription factors and indeed can inhibit transcription factor binding site selectively.

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“…However, we were able to identify in its promoter a binding motif, Yap1p, a protein required for oxidative stress tolerance and also involved in response to cadmium. 54,55 Gis1p is involved in the transcriptional de-repression of genes subjected to the Ras-cAMP dependent GCR mechanism in response to nutrient limitation, 56 whereas Cat8p is involved in the activation of genes required for cell growth in non-fermentable carbon sources. 57 This includes all those genes with mitochondrial functions described above.…”

Section: Regulatory Subnetwork Involved In the Response To The Supple...mentioning

confidence: 99%

Magnesium ions in yeast: setting free the metabolism from glucose catabolite repression

et al. 2016

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In a recent work we showed that magnesium (Mg) plays an important role in industrial ethanol production, overcoming the negative effect of the excess of minerals, particularly copper, present in sugarcane juice, with a consequent increase in ethanol yield. This cation has been reported to be involved in several steps of yeast metabolism, acting mainly as a co-factor of several enzymes of fermentation metabolism and protecting yeast cells from stressful conditions. However, despite many physiological investigations, its effect in the molecular mechanisms that control such metabolic activities remains unclear and to date no information concerning its influence on gene expression has been provided. The present work took advantage of the DNA microarray technology to analyse the global gene expression in yeast cells upon fermentation in Mg-supplemented medium. The results of the fermentation parameters confirmed the previous report on the increase in ethanol yield by Mg. Moreover, the gene expression data revealed an unexpected set of up-regulated genes currently assigned as being negatively-regulated by glucose, which belong to respiratory and energy metabolism, the stress response and the glyoxalate cycle. On the other hand, genes involved in ribosome biogenesis were down-regulated. Computational analysis provided evidence for a regulatory network commanded by key transcriptional factors that may be responsible for the biological action of Mg in yeast cells. In this scenario, Mg seems to act by reprogramming the yeast metabolism by releasing many genes from glucose catabolite repression with positive consequences for ethanol production and maintenance of cell viability.

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Transcriptional activation mediated by the yeast AP-1 protein is required for normal cadmium tolerance.

Cited by 84 publications

References 33 publications

A Genetically Encoded Probe for Cysteine Sulfenic Acid Protein Modification in Vivo

A Genetically Encoded Probe for Cysteine Sulfenic Acid Protein Modification in Vivo

Site-Specific Inhibition of Transcription Factor Binding to DNA by a Metallointercalator

Magnesium ions in yeast: setting free the metabolism from glucose catabolite repression

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