@article {1458,
	title = {Transcription regulation of a yeast gene from a downstream location.},
	journal = {J Mol Biol},
	volume = {425},
	year = {2013},
	month = {2013 Feb 8},
	pages = {457-65},
	abstract = {<p>Mechanisms for coregulation of transcription of tandem genes in yeast remain largely speculative. This study focused on inositol-mediated regulation of the tandem gene pair SNA3-INO1. While the pattern of regulation of these two genes was similar, results showed that intermediate levels of inositol repressed INO1 and induced SNA3. Results also showed that inositol-mediated regulation of the SNA3 gene was not a function of its promoter but occurred from factors within the SNA3-INO1 intergenic region. The basic helix-loop-helix proteins, Ino2p and Ino4p, mediated this regulation through the upstream activation sequence (UAS)(INO) (E-box) sequences in the intergenic region. These results provide a model for studying coregulation of yeast tandem genes. This is especially significant given that many tandem gene pairs in yeast are coregulated even though context-specific UAS sequences are known only for one gene in the pair.</p>
},
	keywords = {Gene Expression Regulation, Fungal, Inositol, Membrane Proteins, Myo-Inositol-1-Phosphate Synthase, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription, Genetic},
	issn = {1089-8638},
	doi = {10.1016/j.jmb.2012.11.018},
	author = {Shetty, Ameet and Swaminathan, Aishwarya and Lopes, John M}
}
@article {31,
	title = {Derepression of INO1 transcription requires cooperation between the Ino2p-Ino4p heterodimer and Cbf1p and recruitment of the ISW2 chromatin-remodeling complex.},
	journal = {Eukaryot Cell},
	volume = {9},
	year = {2010},
	month = {2010 Dec},
	pages = {1845-55},
	abstract = {<p>The Saccharomyces cerevisiae INO1 gene encodes the structural enzyme inositol-3-phosphate synthase for the synthesis de novo of inositol and inositol-containing phospholipids. The transcription of INO1 is completely derepressed in the absence of inositol and choline (I(-) C(-)). Derepression requires the binding of the Ino2p-Ino4p basic helix-loop-helix (bHLH) heterodimer to the UAS(INO) promoter element. We report here the requirement of a third bHLH protein, centromere-binding factor 1 (Cbf1p), for the complete derepression of INO1 transcription. We found that Cbf1p regulates INO1 transcription by binding to sites distal to the INO1 promoter and encompassing the upstream SNA3 open reading frame (ORF) and promoter. The binding of Cbf1p requires Ino2p-Ino4p binding to the UAS(INO) sites in the INO1 promoter and vice versa, suggesting a cooperative mechanism. Furthermore, Cbf1p binding to the upstream sites was required for the binding of the ISW2 chromatin-remodeling complex to the Ino2p-Ino4p-binding sites on the INO1 promoter. Consistent with this, ISW2 was also required for the complete derepression of INO1 transcription.</p>
},
	keywords = {Adenosine Triphosphatases, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Basic Helix-Loop-Helix Transcription Factors, Chromatin, Chromatin Assembly and Disassembly, Dimerization, Gene Expression Regulation, Fungal, Myo-Inositol-1-Phosphate Synthase, Promoter Regions, Genetic, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors, Transcription, Genetic},
	issn = {1535-9786},
	doi = {10.1128/EC.00144-10},
	author = {Shetty, Ameet and Lopes, John M}
}
@article {36,
	title = {Transcriptional regulation of yeast phospholipid biosynthetic genes.},
	journal = {Biochim Biophys Acta},
	volume = {1771},
	year = {2007},
	month = {2007 Mar},
	pages = {310-21},
	abstract = {The last several years have been witness to significant developments in understanding transcriptional regulation of the yeast phospholipid structural genes. The response of most phospholipid structural genes to inositol is now understood on a mechanistic level. The roles of specific activators and repressors are also well established. The knowledge of specific regulatory factors that bind the promoters of phospholipid structural genes serves as a foundation for understanding the role of chromatin modification complexes. Collectively, these findings present a complex picture for transcriptional regulation of the phospholipid biosynthetic genes. The INO1 gene is an ideal example of the complexity of transcriptional control and continues to serve as a model for studying transcription in general. Furthermore, transcription of the regulatory genes is also subject to complex and essential regulation. In addition, databases resulting from a plethora of genome-wide studies have identified regulatory signals that control one of the essential phospholipid biosynthetic genes, PIS1. These databases also provide significant clues for other regulatory signals that may affect phospholipid biosynthesis. Here, we have tried to present a complete summary of the transcription factors and mechanisms that regulate the phospholipid biosynthetic genes.},
	keywords = {CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase, Fungal Proteins, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Intramolecular Lyases, Myo-Inositol-1-Phosphate Synthase, Phospholipids, Saccharomyces cerevisiae Proteins, Transcription Factors, Transcription, Genetic, Yeasts},
	issn = {0006-3002},
	doi = {10.1016/j.bbalip.2006.05.017},
	author = {Chen, Meng and Hancock, Leandria C and Lopes, John M}
}
@article {38,
	title = {Analysis of Opi1p repressor mutants.},
	journal = {Curr Genet},
	volume = {49},
	year = {2006},
	month = {2006 Jan},
	pages = {30-8},
	abstract = {Opi1p is the only known repressor protein specific to the phospholipid biosynthetic pathway. Opi1p is required for repression in response to inositol and choline supplementation. However, the mechanism of Opi1p repression is not completely understood. In part, this is because previously identified opi1 mutants contained nonsense mutations and thus provided little insight into the mechanism of Opi1p function. We have recently reported isolating novel opi1 mutants (rum and dim mutants) that contain missense mutations. Here, we show that these opi1 mutants produce Opi1p product at levels comparable to a wild-type strain. However, these mutants mis-regulate expression of two target genes, INO2-HIS3 and INO1-lacZ, and are also defective in autoregulation. An opi1-S339F mutant is particularly interesting because it completely eliminated autoregulation, but only abated regulation of an INO1-lacZ reporter. Two of the mutations in OPI1 (V343Q and S339F) provide genetic evidence for an interaction between Opi1p and the Ino2p activator since they reside in a region of Opi1p recently shown to interact with Ino2p in vitro. A third mutation (L252F) resides in a region of Opi1p with no known function.},
	keywords = {Amino Acid Sequence, Basic Helix-Loop-Helix Transcription Factors, Conserved Sequence, Molecular Sequence Data, Mutation, Missense, Myo-Inositol-1-Phosphate Synthase, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors},
	issn = {0172-8083},
	doi = {10.1007/s00294-005-0021-6},
	author = {Kaadige, Mohan R and Lopes, John M}
}
