INO1–100: an allele of theSaccharomyces cerevisiae INO1gene that is transcribed without the action of the positive factors encoded by theINO2, INO4, SWI1, SWI2andSWI3genes

Swift, Steven M.; McGraw, Paricia

doi:10.1093/nar/23.8.1426

Cited by 18 publications

(18 citation statements)

References 60 publications

(55 reference statements)

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“…The INO1-100 mutation has been described to be a dominant allele of INO1 lacking 239 bp of the INO1 promoter, including the two UAS INO elements (E1 and E2 in Fig. 4); however, it demonstrates incomplete dominance with respect to INO1 transcription (83). The INO1-100 allele exhibits a nearly constitutive expression of INO1, which is independent of Ino2p and Ino4p (83).…”

Section: Resultsmentioning

confidence: 99%

“…The S. cerevisiae strains used in this study were BY4742 (MAT␣ his3-1 leu2-0 lys2-0 ura3-0); isogenic strains containing the ino2⌬, ino4⌬, pho4⌬, cbf1⌬, sgc1⌬, rtg1⌬, rtg3⌬, hms1⌬, ygr290w⌬, isw2⌬, itc1⌬, isw1⌬, ioc2⌬, ioc3⌬, and ioc4⌬ alleles (30,88); and a strain harboring an INO1 promoter deletion (INO1-100 or OPI5) (66,83). Strains with tandem affinity purification (TAP)-tagged INO2, INO4, CBF1, and ISW2 were purchased from Open Biosystems (Huntsville, AL) (29).…”

Section: Methodsmentioning

confidence: 99%

“…A strain with an INO1 promoter mutant lacking both E boxes and a URS1 element (Ume6p-binding site) (239-bp deletion) was previously denoted INO1-100 (OPI5) (66,83). Two INO1-lacZ reporter plasmids that contained either 1,239 bp of INO1 5Ј-flanking sequences from a wild-type strain or 1,000 bp from the INO1-100 mutant strain were constructed.…”

Section: Methodsmentioning

confidence: 99%

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Derepression ofINO1Transcription Requires Cooperation between the Ino2p-Ino4p Heterodimer and Cbf1p and Recruitment of the ISW2 Chromatin-Remodeling Complex

Shetty

Lopes

2010

Eukaryot Cell

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(11,15,32,39). Most significantly, investigations into its regulation have been driven by the fact that altered INO1 expression is a hallmark of general defects in transcription (35). This study is significant because it reports novel findings regarding new regulators of INO1 transcription.The mechanism for the derepression of INO1 transcription has been extensively studied. Derepression requires the basic helixloop-helix (bHLH) transcription factors Ino2p and Ino4p that bind as a heterodimer to two cis-regulatory (UAS INO ) elements in the INO1 promoter (Fig. 1) (2, 6, 55, 67, 73). The Ino2p activation domain then recruits the Snf1p histone kinase to the INO1 promoter, which phosphorylates Ser10 of histone H3 (62). Phosphorylated histone H3 serves as a docking site for the SAGA acetyltransferase, which acetylates Lys14 on histone H3, but also recruits the TATA-binding protein (TBP) (Fig. 1)

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Derepression ofINO1Transcription Requires Cooperation between the Ino2p-Ino4p Heterodimer and Cbf1p and Recruitment of the ISW2 Chromatin-Remodeling Complex

Shetty

Lopes

2010

Eukaryot Cell

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“…These include mutations in the UME6, SIN3, and RPD3 global repressor genes (Elkhaimi et al 2000). The link between regulation of INO1 gene expression and the Opi À phenotype is further supported by the existence of the dominant OPI51 mutant allele (Swift and McGraw 1995). This mutant is a deletion of the INO1 promoter (renamed the INO1-100 allele), which yields constitutive derepressed expression of the INO1 gene (Swift and McGraw 1995).…”

mentioning

confidence: 99%

“…The link between regulation of INO1 gene expression and the Opi À phenotype is further supported by the existence of the dominant OPI51 mutant allele (Swift and McGraw 1995). This mutant is a deletion of the INO1 promoter (renamed the INO1-100 allele), which yields constitutive derepressed expression of the INO1 gene (Swift and McGraw 1995). 1 Recently, our understanding of the role of Opi1p in the repression of phospholipid biosynthetic gene expression has improved dramatically.…”

mentioning

confidence: 99%

Genomic Analysis of the Opi− Phenotype

2006

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Most of the phospholipid biosynthetic genes of Saccharomyces cerevisiae are coordinately regulated in response to inositol and choline. Inositol affects the intracellular levels of phosphatidic acid (PA). Opi1p is a repressor of the phospholipid biosynthetic genes and specifically binds PA in the endoplasmic reticulum. In the presence of inositol, PA levels decrease, releasing Opi1p into the nucleus where it represses transcription. The opi1 mutant overproduces and excretes inositol into the growth medium in the absence of inositol and choline (Opi À phenotype). To better understand the mechanism of Opi1p repression, the viable yeast deletion set was screened to identify Opi À mutants. In total, 89 Opi À mutants were identified, of which 7 were previously known to have the Opi À phenotype. The Opi À mutant collection included genes with roles in phospholipid biosynthesis, transcription, protein processing/synthesis, and protein trafficking. Included in this set were all nonessential components of the NuA4 HAT complex and six proteins in the Rpd3p-Sin3p HDAC complex. It has previously been shown that defects in phosphatidylcholine synthesis (cho2 and opi3) yield the Opi À phenotype because of a buildup of PA. However, in this case the Opi À phenotype is conditional because PA can be shuttled through a salvage pathway (Kennedy pathway) by adding choline to the growth medium. Seven new mutants present in the Opi À collection ( fun26, kex1, nup84, tps1, mrpl38, mrpl49, and opi10/yol032w) were also suppressed by choline, suggesting that these affect PC synthesis. Regulation in response to inositol is also coordinated with the unfolded protein response (UPR). Consistent with this, several Opi À mutants were found to affect the UPR (yhi9, ede1, and vps74).

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