Relevant bibliographies by topics / Acetate repression

Academic literature on the topic 'Acetate repression'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Acetate repression"

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Toyoda, Koichi, Haruhiko Teramoto, Masayuki Inui, and Hideaki Yukawa. "The ldhA Gene, Encoding Fermentative l-Lactate Dehydrogenase of Corynebacterium glutamicum, Is under the Control of Positive Feedback Regulation Mediated by LldR." Journal of Bacteriology 191, no. 13 (May 1, 2009): 4251–58. http://dx.doi.org/10.1128/jb.00303-09.

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ABSTRACT Corynebacterium glutamicum ldhA encodes l-lactate dehydrogenase, a key enzyme that couples l-lactate production to reoxidation of NADH formed during glycolysis. We previously showed that in the absence of sugar, SugR binds to the ldhA promoter region, thereby repressing ldhA expression. In this study we show that LldR is another protein that binds to the ldhA promoter region, thus regulating ldhA expression. LldR has hitherto been characterized as an l-lactate-responsive transcriptional repressor of l-lactate utilization genes. Transposon mutagenesis of a reporter strain carrying a chromosomal ldhA promoter-lacZ fusion (PldhA-lacZ) revealed that ldhA disruption drastically decreased expression of PldhA-lacZ. PldhA-lacZ expression in the ldhA mutant was restored by deletion of lldR, suggesting that LldR acts as a repressor of ldhA in the absence of l-lactate and the LldR-mediated repression is not relieved in the ldhA mutant due to its inability to produce l-lactate. lldR deletion did not affect PldhA-lacZ expression in the wild-type background during growth on either glucose, acetate, or l-lactate. However, it upregulated PldhA-lacZ expression in the sugR mutant background during growth on acetate. The binding sites of LldR and SugR are located around the −35 and −10 regions of the ldhA promoter, respectively. C. glutamicum ldhA expression is therefore primarily repressed by SugR in the absence of sugar. In the presence of sugar, SugR-mediated repression of ldhA is alleviated, and ldhA expression is additionally enhanced by LldR inactivation in response to l-lactate produced by LdhA.
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Lesley, Joseph A., and Carey D. Waldburger. "Repression of Escherichia coli PhoP-PhoQ Signaling by Acetate Reveals a Regulatory Role for Acetyl Coenzyme A." Journal of Bacteriology 185, no. 8 (April 15, 2003): 2563–70. http://dx.doi.org/10.1128/jb.185.8.2563-2570.2003.

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ABSTRACT The PhoP-PhoQ two-component system regulates the transcription of numerous genes in response to changes in extracellular divalent cation concentration and pH. Here we demonstrate that the Escherichia coli PhoP-PhoQ two-component system also responds to acetate. Signaling by the E. coli PhoP-PhoQ system was repressed during growth in acetate (≥25 mM) in a PhoQ-dependent manner. The periplasmic sensor domain of PhoQ was not required for acetate to repress signaling. Acetate-mediated repression of the PhoP-PhoQ system was not related to changes in the intracellular concentration of acetate metabolites such as acetyl-phosphate or acetyladenylate. Genetic analysis of acetate metabolism pathways suggested that a perturbation of acetyl coenzyme A turnover was the cause of decreased PhoP-PhoQ signaling during growth in acetate. Consistent with this hypothesis, intracellular acetyl coenzyme A levels rose during growth in the presence of exogenous acetate. Acetyl coenzyme A inhibited the autokinase activity of PhoQ in vitro, suggesting that the in vivo repressing effect may be due to a direct inhibition mechanism.
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Shenhar, Galit, and Yona Kassir. "A Positive Regulator of Mitosis, Sok2, Functions as a Negative Regulator of Meiosis in Saccharomyces cerevisiae." Molecular and Cellular Biology 21, no. 5 (March 1, 2001): 1603–12. http://dx.doi.org/10.1128/mcb.21.5.1603-1612.2001.

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ABSTRACT The choice between meiosis and alternative developmental pathways in budding yeast depends on the expression and activity of transcriptional activator Ime1. The transcription of IME1is repressed in the presence of glucose, and a low basal level ofIME1 RNA is observed in vegetative cultures with acetate as the sole carbon source. IREu, a 32-bp element in the IME1promoter, exhibits upstream activation sequence activity depending on Msn2 and -4 and the presence of acetate. We show that in the presence of glucose IREu functions as a negative element and that Sok2 mediates this repression activity. We show that Sok2 associates with Msn2. Sok2 functions as a general repressor whose availability and activity depend on glucose. The activity of Sok2 as a repressor depends on phosphorylation of T598 by protein kinase A (PKA). Relief of repression of Sok2 depends on both the N-terminal domain of Sok2 and Ime1. In the absence of glucose and the presence of Ime1 Sok2 is converted to a weak activator. Overexpression of Sok2 or mild expression of Sok2 with its N-terminal domain deleted leads to a decrease in sporulation. Previously it was reported that overexpression of Sok2 suppresses the growth defect resulting from a temperature-sensitive PKA; thus Sok2 has a positive role in mitosis. We show that Candida albicansEfg1, a homolog of Sok2, complements sok2Δ in repressing IREu. Our results demonstrate that Sok2, a positive regulator of mitosis, and Efg1, a positive regulator of filamentation, function as negative regulators of meiosis. We suggest that cells use the same regulators with opposing effects to ensure that meiosis will be an alternative to mitosis.
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Georgakopoulos, Paraskevi, Robin A. Lockington, and Joan M. Kelly. "SAGA Complex Components and Acetate Repression inAspergillus nidulans." G3: Genes|Genomes|Genetics 2, no. 11 (November 2012): 1357–67. http://dx.doi.org/10.1534/g3.112.003913.

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Ahmed, Hamid K., Wilfrid J. Mitchell, and Fergus G. Priest. "Catabolite repression of histidase biosynthesis inBacillus sphaericusby acetate." FEMS Microbiology Letters 106, no. 1 (January 1993): 71–75. http://dx.doi.org/10.1111/j.1574-6968.1993.tb05937.x.

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6

Kumari, Suman, Christine M. Beatty, Douglas F. Browning, Stephen J. W. Busby, Erica J. Simel, Galadriel Hovel-Miner, and Alan J. Wolfe. "Regulation of Acetyl Coenzyme A Synthetase inEscherichia coli." Journal of Bacteriology 182, no. 15 (August 1, 2000): 4173–79. http://dx.doi.org/10.1128/jb.182.15.4173-4179.2000.

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ABSTRACT Cells of Escherichia coli growing on sugars that result in catabolite repression or amino acids that feed into glycolysis undergo a metabolic switch associated with the production and utilization of acetate. As they divide exponentially, these cells excrete acetate via the phosphotransacetylase-acetate kinase pathway. As they begin the transition to stationary phase, they instead resorb acetate, activate it to acetyl coenzyme A (acetyl-CoA) by means of the enzyme acetyl-CoA synthetase (Acs) and utilize it to generate energy and biosynthetic components via the tricarboxylic acid cycle and the glyoxylate shunt, respectively. Here, we present evidence that this switch occurs primarily through the induction of acs and that the timing and magnitude of this induction depend, in part, on the direct action of the carbon regulator cyclic AMP receptor protein (CRP) and the oxygen regulator FNR. It also depends, probably indirectly, upon the glyoxylate shunt repressor IclR, its activator FadR, and many enzymes involved in acetate metabolism. On the basis of these results, we propose that cells induce acs, and thus their ability to assimilate acetate, in response to rising cyclic AMP levels, falling oxygen partial pressure, and the flux of carbon through acetate-associated pathways.
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Rahman, M. Tanvir, Andrew Crombie, Hélène Moussard, Yin Chen, and J. Colin Murrell. "Acetate Repression of Methane Oxidation by Supplemental Methylocella silvestris in a Peat Soil Microcosm." Applied and Environmental Microbiology 77, no. 12 (April 22, 2011): 4234–36. http://dx.doi.org/10.1128/aem.02902-10.

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ABSTRACTMethylocellaspp. are facultative methanotrophs that grow on methane and multicarbon substrates, such as acetate. Acetate represses transcription of methane monooxygenase ofMethylocella silvestrisin laboratory culture. DNA stable-isotope probing (DNA-SIP) using13C-methane and12C-acetate, carried out withMethylocella-spiked peat soil, showed that acetate also repressed methane oxidation byMethylocellain environmental samples.
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Campbell III, John, Gary R. Bender, and Robert E. Marquis. "Barotolerant variant of Streptococcus faecalis with reduced sensitivity to glucose catabolite repression." Canadian Journal of Microbiology 31, no. 7 (July 1, 1985): 644–50. http://dx.doi.org/10.1139/m85-121.

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Physiological characterization of the APR-11 variant of Streptococcus faecalis ATCC 9790 revealed that the variant has reduced sensitivity to glucose catabolite repression. This reduced sensitivity was indicated by the synthesis of enzymes for catabolism of lactose or arginine in cultures growing at 0.1, 40, or 70 MPa in media with levels of glucose highly repressive for the parent strain. Reduced catabolite repression appeared to be due to reduced activity of the glucose-specific, phosphotransferase system in APR-11 cells. Conversion of pyruvate to lactate or to acetate and ethanol did not appear to be altered in the variant. The APR-11 variant produced a greater final yield of biomass than the parent at all pressures tested, and its barotolerance was especially marked in media with low levels of glucose and high levels of lactose in which derepression of the lactose catabolic system was necessary for full growth. Overall, the greater barotolerance of the APR-11 strain appeared to be due to its enhanced capacity for catabolism related to its reduced sensitivity to catabolite repression by glucose.
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Ampe, Frédéric, David Léonard, and Nicholas D. Lindley. "Repression of Phenol Catabolism by Organic Acids in Ralstonia eutropha." Applied and Environmental Microbiology 64, no. 1 (January 1, 1998): 1–6. http://dx.doi.org/10.1128/aem.64.1.1-6.1998.

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ABSTRACT During batch growth of Ralstonia eutropha (previously named Alcaligenes eutrophus) on phenol in the presence of acetate, acetate was found to be the preferred substrate; this organic acid was rapidly metabolized, and the specific rate of phenol consumption was considerably decreased, although phenol consumption was not abolished. This decrease corresponded to a drop in phenol hydroxylase and catechol-2,3-dioxygenase specific activities, and the synthesis of the latter was repressed at the transcriptional level. Studies with a mutant not able to consume acetate indicated that the organic acid itself triggers the repression. Other organic acids were also found to repress phenol degradation. One of these, benzoate, was found to completely block the catabolism of phenol (diauxic growth). A mutant unable to metabolize benzoate was also unable to develop on benzoate-phenol mixtures, indicating that the organic acid rather than a metabolite involved in benzoate degradation was responsible for the repression observed.
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Haas, MJ, D. Reinacher, JP Li, NC Wong, and AD Mooradian. "Regulation of apoA1 gene expression with acidosis: requirement for a transcriptional repressor." Journal of Molecular Endocrinology 27, no. 1 (August 1, 2001): 43–57. http://dx.doi.org/10.1677/jme.0.0270043.

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Serum apolipoprotein A(1) (apoA(1)) concentration is inversely correlated with the risk of premature atherosclerosis. Serum apoA(1) concentrations are regulated, in part, at the transcriptional level. ApoA(1) mRNA is synthesized primarily in the liver and small intestine, under the direction of a number of signaling molecules and tissue-specific regulatory elements. Previously, we demonstrated that extracellular acidosis suppresses apoA(1) mRNA levels at the level of transcription. Here we demonstrate that intracellular acidosis, in the absence of extracellular pH changes, represses apoA(1) promoter activity. Repression occurs through a pH responsive element (pH-RE) located within the apoA(1) gene promoter. Acidosis increases the specific DNA binding activity of a putative repressor protein within the immediate 5'-flanking region of the apoA(1) gene. The cis-element that binds the putative repressor protein contains a negative thyroid hormone response element (nTRE) located 3' and adjacent to the apoA(1) TATA box. Mutation of the nTRE/pH-RE abrogates protein binding and alters the activity of reporter genes controlled by this element. Repression by acidosis did not require de novo mRNA and protein synthesis. Inhibition of tyrosine kinase activity and diacylglycerol-stimulated protein kinase C (PKC) signaling pathways with tyrophostin A47 and phorbol myristate acetate, respectively, did not affect the repression of apoA(1) promoter activity with acidosis. These results suggest that transcriptional repression of the apoA(1) gene by alterations in ambient pH is associated with enhanced DNA binding activity of a repressor protein, through a mechanism which appears to be independent of de novo mRNA and protein synthesis, tyrosine kinase activity, or PKC activation.
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Dissertations / Theses on the topic "Acetate repression"

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Benevides, Kristina, Oscar Broström, Kalman Grim Elison, Hugo Swenson, Andrei Vlassov, and Josefin Ågren. "Stabil och antibiotikafri läkemedelsproduktion i rekombinant Escherichia coli." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-323719.

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Den här rapporten presenterar ett antibiotikafritt, stabilt och kromosombaserat expressionssystem för läkemedelsproduktion i Escherichia coli på beställning av företaget Affibody AB. E. coli-stammen BL21(DE3) valdes som värdorganism för expressionssystemet. Systemet består av en genkassett som innehåller en T7-promotor, en 5′-UTR från genen ompA och en terminatorsekvens från RNA-operonet rrnB. Fyra kopior av genkassetten ska integreras i pseudogenerna caiB, yjjM, hsdS och yjiV. En datormodell som modellerar det egentliga kopietalet i cellerna har skapats i mjukvaran MATLAB, vilket visar att det uppskattas vara maximalt 32 kopior av genkassetten per cell på grund av replikation av kromosomen. Ett högt pH i fermentorn; att använda fed-batch och blandade kolhydratkällor; och att använda stammen BL21(DE3) minskar acetatproduktionen i cellen. En lägre acetatproduktion kan leda till en högre produkthalt. En proteinutbytesmodell för mjukvaran MATLAB har konstruerats för att uppskatta koncentrationen av Affibody®-molekylen i en E. coli cell.
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2

Georgakopoulos, Paraskevi. "Regulation of carbon catabolite repression in the filamentous fungus Aspergillus nidulans." Thesis, 2012. http://hdl.handle.net/2440/82441.

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In Aspergillus nidulans, acetate is a repressing carbon source that leads to similar levels of CreA mediated repression as glucose. acdX was identified in a mutation screen in Aspergillus nidulans to identify genes involved in acetate repression but not in glucose repression. The conservation of the amino acid sequence of AcdX of A. nidulans and Spt8 of Saccharomyces cerevisiae suggests that the SAGA (Spt-Ada-Gcn5-Acetyltransferase) complex may have a role in acetate repression in A. nidulans, since Spt8 is a component of the SAGA complex. We also made mutations in sptC, homologous to the yeast SAGA component gene SPT3, which show a similar phenotype to the acdX mutants. The SAGA complex is highly conserved from yeast to humans. In yeast it is involved mostly in the regulation of highly regulated genes that respond to environmental stresses, such as metabolic starvation, DNA damage and heat. SAGA in yeast has been shown to have positive and negative functions on transcription. Bioinformatic analysis indicates that the components of the SAGA complex are also present in A. nidulans. CreA has been shown to repress the expression of the alc regulon, which is required for the ethanol utilization pathway. Although plate tests indicated that acdX and sptC null mutations led to derepressed alcohol dehydrogensed activity, RT-qPCR showed no derepression of alcA or aldA, but rather elevated induced levels. Our results indicate that acetate repression is due to repression via CreA together with metabolic changes, rather than due to an independent regulatory control mechanism. Furthermore experiments were undertaken to confirm the existence of the SAGA complex in A. nidulans. SptC was N terminally tagged with the TAP tag to allow the purification of the SAGA complex. Proteomic analysis indicates that the SAGA complex does exist in A.nidulans, although there are some differences, one of which is that it lacks the deubiquitinating subgroup.
Thesis (Ph.D.) -- University of Adelaide, School of Molecular and Biomedical Science, 2012
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