Constitutive expression of yeast phospholipid biosynthetic genes by variants of Ino2 activator defective for interaction with Opi1 repressor

Heyken, Willm‐Thomas; Repenning, Antje; Kumme, Jacqueline; Schüller, Hans‐Joachim

doi:10.1111/j.1365-2958.2004.04499.x

Cited by 59 publications

(69 citation statements)

References 43 publications

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“…INO2 and INO4 were also required for full expression of the RTG3-cat gene in a ρ 0 strain ( Figure 6B). It has been previously shown that inositol-mediated regulation of INO2 expression requires both INO2 and INO4 Lopes, 1995a, 1995b;Eiznhamer et al, 2001;Gardenour et al, 2004;Heyken et al, 2005;Jackson and Lopes, 1996;Miller and Lopes, 2001;Schwank et al, 1997). Similarly, RTG3-cat expression was induced in a ρ 0 strain which supports previously published results (Figure 6) (Jia et al, 1997).…”

Section: Discussionsupporting

confidence: 90%

“…Interestingly, deletion of the PHO4 gene did not eliminate phosphate regulation of RTG3-cat (Figure 6). Lastly, deletion of RTG3 and RTG1 did not significantly affect RTG3-cat expression, suggesting that RTG3 does not autoregulate its expression, as has been shown for the INO2 gene Lopes, 1995a, 1995b;Eiznhamer et al, 2001;Gardenour et al, 2004;Heyken et al, 2005;Miller and Lopes, 2001;Schwank et al, 1997) and other bHLH-encoding genes (Shetty, He, Chen and Lopes, unpublished data).…”

Section: Rtg3 Expression Is Also Regulated By Bhlh Proteinsmentioning

confidence: 56%

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Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

Chen¹,

Lopes²

2010

Yeast

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The basic helix-loop-helix (bHLH) proteins comprise a eukaryotic transcription factor family involved in multiple biological processes. They have the ability to form multiple dimer combinations and most of them also bind a 6 bp site (E-box) with limited specificity. These properties make them ideal for combinatorial regulation of gene expression. The Saccharomyces cerevisiae CIT2 gene, which encodes citrate synthase, was previously known to be induced by the bHLH proteins Rtg1p and Rtg3p in response to mitochondrial damage. Rtg1p-Rtg3p dimers bind two R-boxes (modified E-boxes) in the CIT2 promoter. The current study tested the ability of all nine S. cerevisiae bHLH proteins to regulate the CIT2 gene. The results showed that expression of CIT2-lacZ reporter was induced in a ρ 0 strain by the presence of inositol via the Ino2p and Ino4p bHLH proteins, which are known regulators of phospholipid synthesis. Promoter mutations revealed that inositol induction required a distal E-box in the CIT2 promoter. Interestingly, deleting the INO2, INO4 genes or the cognate E-box revealed phosphate induction of CIT2 expression. This layer of expression required the two R-boxes and the Pho4p bHLH protein, which is known to be required for phosphate-specific regulation. Lastly, the data show that the Hms1p and Sgc1p bHLH proteins also play important roles in repression of CIT2-lacZ expression. Collectively, these results support the model that yeast bHLH proteins coordinate different biological pathways.

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Section: Discussionsupporting

confidence: 90%

Section: Rtg3 Expression Is Also Regulated By Bhlh Proteinsmentioning

confidence: 56%

Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

Chen¹,

Lopes²

2010

Yeast

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“…Meanwhile, both INO80 and SWI/SNF are also present at the promoter. Although the transcriptional activator and chromatin remodelers are present at the promoter under repressing conditions, the transcriptional activator is quiescent in the presence of Opi1p [15]. The remodelers remain inactive and the chromatin is in a static state.…”

Section: Discussionmentioning

confidence: 99%

“…This regulation is controlled by the cis-acting promoter element UAS INO [9,10], which is the binding site for the heterodimeric transcriptional activator, Ino2p/Ino4p [11,12]. Despite the constitutive binding of Ino2p/Ino4p to UAS INO [13,14], inositol suppresses transcriptional activation via Opi1p, which mediates repression through its activator interaction domain, by binding to the repressor interaction domain of Ino2p [15].…”

Section: Introductionmentioning

confidence: 99%

Activator-dependent recruitment of SWI/SNF and INO80 during INO1 activation

Ford¹,

Odeyale²,

Shen³

2008

Biochemical and Biophysical Research Communications

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Transcriptional activation of yeast INO1 requires SWI/SNF and INO80 for nucleosome disruption at the promoter. However, the cooperative interplay among remodelers and their recruitment dynamics in activation have thus far been vague. Here, we showed, using chromatin immunoprecipitation, that both SWI/SNF and INO80 are present at the promoter and are restricted to the promoter, indicating that they directly participate in localized INO1 chromatin remodeling. Furthermore, both SWI/SNF and INO80 are absent at the INO1 promoter in ino2Δ cells, suggesting that these are activator-dependent remodelers. We have also found that the presence of INO80 is required for SWI/SNF recruitment, indicating that INO80 arrives first at the promoter followed by SWI/SNF. In light of these findings, we proposed a model which describes the order of events in INO1 activation.

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“…Nonetheless, despite the continual binding of Ino2p/Ino4p to UAS INO , inositol suppresses transcriptional activation via the Opi1p repressor. Opi1p mediates repression via its activator interaction domain, which binds to the repressor interaction domain of Ino2p (10)(11)(12).…”

Section: Introductionmentioning

confidence: 99%

A SWI/SNF- and INO80-dependent nucleosome movement at the INO1 promoter

Ford

Odeyale

Eskandar

et al. 2007

Biochemical and Biophysical Research Communications

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Transcriptional activation in yeast INO1 chromatin was studied using the indirect end-labeling technique. INO1 chromatin is organized into an ordered, overlapping nucleosomal array under repressing conditions. Nucleosome positions were only disrupted at the promoter region under inducing conditions in the presence of SWI/SNF and INO80. Mutants lacking either remodeler demonstrated identical positioning patterns as the wild type under repressing conditions. This indicates that these two remodelers are responsible and essential for local nucleosomal mobilization at the INO1 promoter. The area of local nucleosome movement is consistent with the previously identified region of histone deacetylation activity. In light of these findings, we suggest that nucleosomes subject to local mobilization are also targets for local histone modifications.

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Constitutive expression of yeast phospholipid biosynthetic genes by variants of Ino2 activator defective for interaction with Opi1 repressor

Cited by 59 publications

References 43 publications

Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

Activator-dependent recruitment of SWI/SNF and INO80 during INO1 activation

A SWI/SNF- and INO80-dependent nucleosome movement at the INO1 promoter

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