The yeast gene <i>YJR025c</i> encodes a 3‐hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis

Kucharczyk, Róża; Zagulski, Marek; Rytka, Joanna; Herbert, Christopher J.

doi:10.1016/s0014-5793(98)00153-7

Cited by 52 publications

(44 citation statements)

References 12 publications

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“…1, AGA1 and SGA1 are alpha-factor induced; INO1, GND2, YDR533C, YGR043C, and YHR087W are all induced by alphafactor and during the diauxic shift, TSL1 is a stress-induced gene also activated during the diauxic shift, and HSP26 is activated by stress, alpha-factor, and during the diauxic shift (17,21). Interestingly, BNA1 encodes a component of the de novo synthesis pathway for nicotinic acid; altered levels of nicotinic acid could influence the levels of SIR2's NAD-dependent histone deacetylase activity (26,27) and thereby activate expression of genes involved in mating and sporulation (27). To test this idea, message levels in the mot1-14 strain were compared with those in wild-type BNA1 and bna1⌬ strains.…”

Section: Correlations With Other Transcriptional Regulators and The Dmentioning

confidence: 99%

Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms

Dasgupta

Darst²,

Martin³

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

134

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Mot1 is an essential yeast Snf2/Swi2-related ATPase that exerts both positive and negative effects on gene expression. In vitro, Mot1 can disrupt TATA-binding protein–DNA complexes in an ATP-dependent reaction. This activity can explain Mot1-mediated transcriptional repression, but how Mot1 activates transcription is unknown. We demonstrate that, remarkably, Mot1 is localized in vivo to promoters for both Mot1-repressed and Mot1-activated genes. Moreover, Mot1 ATPase activity is required for both activation and repression of gene activity. These findings suggest a novel function for the Mot1 ATPase at activated genes, perhaps involving ATP-driven reorganization of the preinitiation complex. Mot1 regulates the expression of ≈3% of yeast genes in cells grown in rich medium. Most of these genes are repressed by Mot1, consistent with Mot1's ATP-dependent TATA-binding protein–DNA dissociating activity. Additionally, ≈77% of the Mot1-repressed genes are involved in the diauxic shift, stress response, mating, or sporulation. The gene sets controlled by NC2 and Srb10 are strongly correlated with the Mot1-controlled set, suggesting that these factors cooperate in transcriptional control on a global scale

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Section: Correlations With Other Transcriptional Regulators and The Dmentioning

confidence: 99%

Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms

Dasgupta

Darst²,

Martin³

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

134

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“…As controls, we tested the effects of deleting BNA1 or TNA1, which does not reduce the NAD ϩ concentration or (51). Deleting BNA1 blocks the de novo NAD ϩ biosynthesis pathway (26), and deleting TNA1 reduces nicotinic acid import from the growth medium (33). To assess the global transcriptional responses under each of these conditions, we grew the WT, npt1⌬, pnc1⌬, bna1⌬, and tna1⌬ strains in YPD medium.…”

Section: Resultsmentioning

confidence: 99%

“…NAD ϩ is synthesized de novo in multiple enzymatic steps carried out by the Bna1-Bna6 proteins to synthesize nicotinic acid mononucleotide (NaMN) (26), which is then converted to NAD ϩ by the adenylyltransferases Nma1 and Nma2 (1) and then NAD synthetase (Qns1) (6) (Fig. 1A).…”

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confidence: 99%

Thiamine Biosynthesis in Saccharomyces cerevisiae Is Regulated by the NAD⁺-Dependent Histone Deacetylase Hst1

Petteys

McClure

et al. 2010

Molecular and Cellular Biology

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Genes encoding thiamine biosynthesis enzymes in microorganisms are tightly regulated such that low environmental thiamine concentrations activate transcription and high concentrations are repressive. We have determined that multiple thiamine (THI) genes in Saccharomyces cerevisiae are also regulated by the intracellular NAD ؉ concentration via the NAD ؉ -dependent histone deacetylase (HDAC) Hst1 and, to a lesser extent, Sir2. Both of these HDACs associate with a distal region of the affected THI gene promoters that does not overlap with a previously defined enhancer region bound by the thiamine-responsive Thi2/Thi3/Pdc2 transcriptional activators. The specificity of histone H3 and/or H4 deacetylation carried out by Hst1 and Sir2 at the distal promoter region depends on the THI gene being tested. Hst1/Sir2-mediated repression of the THI genes occurs at the level of basal expression, thus representing the first set of transcription factors shown to actively repress this gene class. Importantly, lowering the NAD ؉ concentration and inhibiting the Hst1/Sum1 HDAC complex elevated the intracellular thiamine concentration due to increased thiamine biosynthesis and transport, implicating NAD ؉ in the control of thiamine homeostasis.

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“…The consumption of NAD 1 implies there is a constant need for NAD known pathways (see Figure 1A for schematic). The de novo NAD 1 synthesis pathway converts tryptophan into NAD 1 through a series of steps also known as the kynurenine pathway that are catalyzed by products of the BNA genes (Kucharczyk et al 1998). This pathway is cytosolic and does not usually contribute to rDNA silencing regulation unless nicotinic acid in the growth medium is limiting (Anderson et al 2002;Sandmeier et al 2002).…”

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confidence: 99%

Pnc1p-Mediated Nicotinamide Clearance Modifies the Epigenetic Properties of rDNA Silencing in Saccharomyces cerevisiae

McClure

Gallo²,

Smith

et al. 2008

Genetics

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The histone deacetylase activity of Sir2p is dependent on NAD 1 and inhibited by nicotinamide (NAM). As a result, Sir2p-regulated processes in Saccharomyces cerevisiae such as silencing and replicative aging are susceptible to alterations in cellular NAD 1 and NAM levels. We have determined that high concentrations of NAM in the growth medium elevate the intracellular NAD 1 concentration through a mechanism that is partially dependent on NPT1, an important gene in the Preiss-Handler NAD 1 salvage pathway. Overexpression of the nicotinamidase, Pnc1p, prevents inhibition of Sir2p by the excess NAM while maintaining the elevated NAD 1 concentration. This growth condition alters the epigenetics of rDNA silencing, such that repression of a URA3 reporter gene located at the rDNA induces growth on media that either lacks uracil or contains 5-fluoroorotic acid (5-FOA), an unusual dual phenotype that is reminiscent of telomeric silencing (TPE) of URA3. Despite the similarities to TPE, the modified rDNA silencing phenotype does not require the SIR complex. Instead, it retains key characteristics of typical rDNA silencing, including RENT and Pol I dependence, as well as a requirement for the Preiss-Handler NAD 1 salvage pathway. Exogenous nicotinamide can therefore have negative or positive impacts on rDNA silencing, depending on the PNC1 expression level.

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The yeast gene YJR025c encodes a 3‐hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis

Cited by 52 publications

References 12 publications

Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms

Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms

Thiamine Biosynthesis in Saccharomyces cerevisiae Is Regulated by the NAD⁺-Dependent Histone Deacetylase Hst1

Pnc1p-Mediated Nicotinamide Clearance Modifies the Epigenetic Properties of rDNA Silencing in Saccharomyces cerevisiae

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The yeast gene YJR025c encodes a 3‐hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis

Cited by 52 publications

References 12 publications

Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms

Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms

Thiamine Biosynthesis in Saccharomyces cerevisiae Is Regulated by the NAD+-Dependent Histone Deacetylase Hst1

Pnc1p-Mediated Nicotinamide Clearance Modifies the Epigenetic Properties of rDNA Silencing in Saccharomyces cerevisiae

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Thiamine Biosynthesis in Saccharomyces cerevisiae Is Regulated by the NAD⁺-Dependent Histone Deacetylase Hst1