scholarly journals Arginine-specific repression in Saccharomyces cerevisiae: kinetic data on ARG1 and ARG3 mRNA transcription and stability support a transcriptional control mechanism.

1990 ◽  
Vol 10 (3) ◽  
pp. 1226-1233 ◽  
Author(s):  
M Crabeel ◽  
R Lavalle ◽  
N Glansdorff
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Translational Regulation ◽  
Transcriptional Control ◽  
Time Course ◽  
Regulatory Proteins ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Mrna Transcription ◽  
Steady State Levels ◽  
Kinetics Of

A specific repression mechanism regulates arginine biosynthesis in Saccharomyces cerevisiae. The involvement of regulatory proteins displaying DNA-binding features and the location of an operator region between the TATA box and the transcription start of the structural gene ARG3 suggest that this mechanism operates at the level of transcription. A posttranscriptional mechanism has, however, been proposed to account for the conspicuous lack of proportionality between ARG3 mRNA steady-state levels (as determined by Northern [RNA] assays; F. Messenguy and E. Dubois, Mol. Gen. Genet. 189:148-156, 1983) and the cognate enzyme activities. In this work, we have analyzed the time course of the incorporation of radioactive precursors into ARG1 and ARG3 mRNAs and the kinetics of their decay under different regulatory statuses. The results (expressed in terms of relative mRNA levels, relative transcription rates, and mRNA half-lives) give the picture expected from a purely transcriptional control. A similar analysis of expression of the gene CPA1, for which a translational regulation by arginine has been clearly demonstrated (M. Werner, A. Feller, F. Messenguy, and A. Piérard, Cell 49:805-813, 1987), indicates that this gene is also partly regulated at the transcriptional level by the ARGR repressor system. Moreover, the half-life of CPA1 mRNA is reduced twofold in the presence of excess arginine; we suggest that this could be inherent in the mechanism of translational regulation of CPA1.

Arginine-specific repression in Saccharomyces cerevisiae: kinetic data on ARG1 and ARG3 mRNA transcription and stability support a transcriptional control mechanism

1990 ◽  
Vol 10 (3) ◽  
pp. 1226-1233
Author(s):  
M Crabeel ◽  
R Lavalle ◽  
N Glansdorff
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Translational Regulation ◽  
Transcriptional Control ◽  
Time Course ◽  
Regulatory Proteins ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Mrna Transcription ◽  
Steady State Levels ◽  
Kinetics Of

A specific repression mechanism regulates arginine biosynthesis in Saccharomyces cerevisiae. The involvement of regulatory proteins displaying DNA-binding features and the location of an operator region between the TATA box and the transcription start of the structural gene ARG3 suggest that this mechanism operates at the level of transcription. A posttranscriptional mechanism has, however, been proposed to account for the conspicuous lack of proportionality between ARG3 mRNA steady-state levels (as determined by Northern [RNA] assays; F. Messenguy and E. Dubois, Mol. Gen. Genet. 189:148-156, 1983) and the cognate enzyme activities. In this work, we have analyzed the time course of the incorporation of radioactive precursors into ARG1 and ARG3 mRNAs and the kinetics of their decay under different regulatory statuses. The results (expressed in terms of relative mRNA levels, relative transcription rates, and mRNA half-lives) give the picture expected from a purely transcriptional control. A similar analysis of expression of the gene CPA1, for which a translational regulation by arginine has been clearly demonstrated (M. Werner, A. Feller, F. Messenguy, and A. Piérard, Cell 49:805-813, 1987), indicates that this gene is also partly regulated at the transcriptional level by the ARGR repressor system. Moreover, the half-life of CPA1 mRNA is reduced twofold in the presence of excess arginine; we suggest that this could be inherent in the mechanism of translational regulation of CPA1.

Gene expression after resumption of development of Artemia franciscana cryptobiotic embryos

1994 ◽  
Vol 72 (3-4) ◽  
pp. 78-83 ◽  
Author(s):  
Ricardo Escalante ◽  
Alberto García-Sáez ◽  
Maria-Asunción Ortega ◽  
Leandro Sastre
Keyword(s):  
Gene Expression ◽  
Time Course ◽  
Developmental Stages ◽  
Artemia Franciscana ◽  
Mrna Levels ◽  
Muscle Actin ◽  
Mrna Accumulation ◽  
Α Subunit ◽  
Steady State Levels ◽  
Cyst Development

The steady-state levels of six different mRNAs have been studied during Artemia franciscana development. Some of these mRNAs are present in the cryptobiotic cyst, like those coding for cytoplasmic actins, sarcoplasmic/endoplasmic reticulum Ca2+-ATPase, and the Na+,K+-ATPase α-subunit isoform coded by the clone pArATNa136. The expression of these mRNAs is markedly induced during cyst development. A small increase in mRNA levels can be observed for some genes at very early stages of development (2 h). The main increase is observed between 4 and 16 h of development for all these genes, although the time course of mRNA accumulation is different for each one of the genes studied. Some other genes, like those coding for muscle actin (actin 3) or the Na+,K+-ATPase α-subunit isoform coded by the cDNA clone α2850, are not expressed in the cyst before resumption of development and their expression is induced after 10 or 6 h of development, respectively. These data on the kinetic of mRNA accumulation provide the information required to determine transcriptionally active developmental stages, necessary to study in more detail the mechanisms of transcriptional regulation during activation of cryptobiotic cysts and resumption of embryonic development.Key words: Artemia, gene expression, actin, Na,K-ATPase, Ca2+-ATPase.

scholarly journals Negative regulatory gene for general control of amino acid biosynthesis in Saccharomyces cerevisiae.

1986 ◽  
Vol 6 (9) ◽  
pp. 3150-3155 ◽  
Author(s):  
P L Myers ◽  
R C Skvirsky ◽  
M L Greenberg ◽  
H Greer
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Regulatory Gene ◽  
Negative Regulator ◽  
Single Amino Acid ◽  
Mrna Levels ◽  
General Control ◽  
Biosynthetic Genes ◽  
Isolation And Characterization ◽  
Steady State Levels

In Saccharomyces cerevisiae, many amino acid biosynthetic pathways are coregulated by a complex general control system: starvation for a single amino acid results in the derepression of amino acid biosynthetic genes in multiple pathways. Derepression of these genes is mediated by positive (GCN) and negative (GCD) regulatory genes. In this paper we describe the isolation and characterization of a previously unreported negative regulatory gene, GCD3. A gcd3 mutation is recessive to wild type, confers resistance to multiple amino acid analogs, and results in overproduction and partially constitutive elevation of mRNA levels for amino acid biosynthetic genes. Furthermore, a gcd3 mutation can overcome the derepression-deficient phenotype of mutations in the positive regulatory GCN1, GCN2, and GCN3 genes. However, the gcd3 mutation cannot overcome the derepression-deficient phenotype of a gcn4 mutation, suggesting that GCD3 acts as a negative regulator of the important GCN4 gene. Northern blot analysis confirmed this conclusion, in that the steady-state levels of GCN4 mRNA are greatly increased in a gcd3 mutant. Thus, the negative regulatory gene GCD3 plays a central role in derepression of amino acid biosynthetic genes.

scholarly journals Localization and Interaction of the Proteins Constituting the GAL Genetic Switch in Saccharomyces cerevisiae

2008 ◽  
Vol 7 (12) ◽  
pp. 2061-2068 ◽  
Author(s):  
Raymond Wightman ◽  
Rachel Bell ◽  
Richard J. Reece
Keyword(s):  
Gene Expression ◽  
Saccharomyces Cerevisiae ◽  
Cellular Localization ◽  
Transcriptional Control ◽  
Resonance Energy ◽  
Regulatory Proteins ◽  
Yeast Cells ◽  
Galactose Metabolism ◽  
Genetic Switch ◽  
Metabolism Regulation

ABSTRACT In Saccharomyces cerevisiae, the GAL genes encode the enzymes required for galactose metabolism. Regulation of these genes has served as the paradigm for eukaryotic transcriptional control over the last 50 years. The switch between inert and active gene expression is dependent upon three proteins—the transcriptional activator Gal4p, the inhibitor Gal80p, and the ligand sensor Gal3p. Here, we present a detailed spatial analysis of the three GAL regulatory proteins produced from their native genomic loci. Using a novel application of photobleaching, we demonstrate, for the first time, that the Gal3p ligand sensor enters the nucleus of yeast cells in the presence of galactose. Additionally, using Förster resonance energy transfer, we show that the interaction between Gal3p and Gal80p occurs throughout the yeast cell. Taken together, these data challenge existing models for the cellular localization of the regulatory proteins during the induction of GAL gene expression by galactose and suggest a mechanism for the induction of the GAL genes in which galactose-bound Gal3p moves from the cytoplasm to the nucleus to interact with the transcriptional inhibitor Gal80p.

Transcriptional and post-transcriptional control of PHO8 expression by PHO regulatory genes in Saccharomyces cerevisiae

1985 ◽  
Vol 5 (1) ◽  
pp. 248-252
Author(s):  
Y Kaneko ◽  
Y Tamai ◽  
A Toh-e ◽  
Y Oshima
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alkaline Phosphatase ◽  
Genetic Study ◽  
Transcriptional Control ◽  
Regulatory Genes ◽  
Transcriptional Level ◽  
Dna Fragment ◽  
Phosphate Medium ◽  
High Phosphate ◽  
In Cells

A DNA fragment bearing the PHO8 gene, which encodes repressible alkaline phosphatase of Saccharomyces cerevisiae, was cloned. Northern hybridizations with the PHO8 DNA as probe indicated that the PHO8 transcript is 1.8 kilobases in length and is more abundant in cells grown in low-phosphate medium than in high-phosphate medium. The pho9 mutant, whose phenotype is defective in the activity of repressible alkaline phosphatase, produced as much of the PHO8 transcript as did the PHO9+ cells. Hence, the PHO9 product should act at the post-transcriptional level. The pho4 mutant could not derepress the PHO8 transcript, whereas the pho80 mutant could, irrespective of the amount of Pi in the medium, as has been suggested by genetic study.

Effects of Sialagogues on Ornithine Decarboxylase Induction and Proto-oncogene Expression in Murine Parotid Gland

1992 ◽  
Vol 71 (12) ◽  
pp. 1885-1890 ◽  
Author(s):  
M. Kawano ◽  
A. Ueno ◽  
Y. Ashida ◽  
N. Matsumoto ◽  
H. Inoue
Keyword(s):  
Parotid Gland ◽  
Ornithine Decarboxylase ◽  
Transcriptional Control ◽  
Polymyxin B ◽  
Transcriptional Level ◽  
Level 3 ◽  
Steady State Levels ◽  
Rat Parotid

The mechanism of a sialagogue-induced increase in ornithine decarboxylase (ODC) activity and the expressions of proto-oncogenes in murine parotid gland were investigated by use of isoproterenol (IPR), carbachol (CC), and methoxamine (MTX). The results were as follows: (1) The three sialagogues had similar effects on the parotid in vivo (mouse parotid after a single injection of IPR) and/or in vitro (rat parotid explants cultured on siliconized lens paper floating on 199 medium containing IPR, CC, or MTX), the order of their effectiveness being IPR > CC > MTX. (2) Northern/dot and Western blot analyses revealed that the sialagogues elevated the steady-state levels of ODC mRNA and ODC protein to maxima at two h and six h, respectively, after stimulation. The increases were roughly proportional to those in ODC activity, suggesting that sialagogue-dependent enzyme induction is regulated at the transcriptional level. (3) The mRNAs of four of nine proto-oncogenes examined showed sialagogue-dependent increases to maxima at 30 min (c-fos) or 60 min (c-jun, c-myc, and c-src) after the beginning of stimulation. These increases were all transient, with the levels returning to the control values (without sialagogue) within 60 min. (4) The IPR-dependent elevations of ODC activity and the mRNAs of ODC, c-fos, and c -jun were inhibited by monensin, but not by polymyxin B. On the other hand, the CC-dependent increases in these parameters were inhibited by polymyxin B but not by monensin. The IPR- and CC-induced increases in c-myc and c-src mRNAs were not inhibited by either monensin or polymyxin B, suggesting that the c-Fos and c-Jun proteins participate in this transcriptional control through the AP-1 site of the ODC gene.

scholarly journals Transcriptional and post-transcriptional control of PHO8 expression by PHO regulatory genes in Saccharomyces cerevisiae.

1985 ◽  
Vol 5 (1) ◽  
pp. 248-252 ◽  
Author(s):  
Y Kaneko ◽  
Y Tamai ◽  
A Toh-e ◽  
Y Oshima
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alkaline Phosphatase ◽  
Genetic Study ◽  
Transcriptional Control ◽  
Regulatory Genes ◽  
Transcriptional Level ◽  
Dna Fragment ◽  
Phosphate Medium ◽  
High Phosphate ◽  
In Cells

A DNA fragment bearing the PHO8 gene, which encodes repressible alkaline phosphatase of Saccharomyces cerevisiae, was cloned. Northern hybridizations with the PHO8 DNA as probe indicated that the PHO8 transcript is 1.8 kilobases in length and is more abundant in cells grown in low-phosphate medium than in high-phosphate medium. The pho9 mutant, whose phenotype is defective in the activity of repressible alkaline phosphatase, produced as much of the PHO8 transcript as did the PHO9+ cells. Hence, the PHO9 product should act at the post-transcriptional level. The pho4 mutant could not derepress the PHO8 transcript, whereas the pho80 mutant could, irrespective of the amount of Pi in the medium, as has been suggested by genetic study.

scholarly journals Yeh1 Constitutes the Major Steryl Ester Hydrolase under Heme-Deficient Conditions in Saccharomyces cerevisiae

2006 ◽  
Vol 5 (7) ◽  
pp. 1018-1025 ◽  
Author(s):  
René Köffel ◽  
Roger Schneiter
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acids ◽  
Steady State ◽  
Rna Polymerase Ii ◽  
Lipid Droplets ◽  
Transcriptional Control ◽  
Steryl Ester ◽  
Unsaturated Fatty Acids ◽  
Ester Hydrolase ◽  
Steady State Levels

ABSTRACT Steryl esters are stored in intracellular lipid droplets from which they are mobilized upon demand and hydrolyzed to yield free sterols and fatty acids. The mechanisms that control steryl ester mobilization are not well understood. We have previously identified a family of three lipases of Saccharomyces cerevisiae that are required for efficient steryl ester hydrolysis, Yeh1, Yeh2, and Tgl1 (R. Köffel, R. Tiwari, L. Falquet, and R. Schneiter, Mol. Cell. Biol. 25:1655-1668, 2005). Both Yeh1 and Tgl1 localize to lipid droplets, whereas Yeh2 is localized to the plasma membrane. To characterize the precise function of these three partially redundant lipases, we examined steryl ester mobilization under heme-deficient conditions. S. cerevisiae is a facultative anaerobic organism that becomes auxotrophic for sterols and unsaturated fatty acids in the absence of molecular oxygen. Anaerobic conditions can be mimicked in cells that are deficient for heme synthesis. We here report that Yeh1 is the sole active steryl ester hydrolase under such heme-deficient conditions, indicating that Yeh1 is activated whereas Yeh2 and Tgl1 are inactivated by the lack of heme. The heme-dependent activation of Yeh1 is mediated at least in part by an increase in steady-state levels of Yeh1 at the expense of Yeh2 and Tgl1 in exponentially growing cells. This increase in steady-state levels of Yeh1 requires Rox3, a component of the mediator complex that regulates transcription by RNA polymerase II. These data thus provide the first link between fat degradation and the transcriptional control of lipase activity in yeast.

scholarly journals A Novel Role of PM Extracts on the Post-Transcriptional Control of Pro-Inflammatory Mediators, IL-6 and CXCL8

Atmosphere ◽  
2019 ◽  
Vol 10 (5) ◽  
pp. 270
Author(s):  
Evasomary Rivera-Ramírez ◽  
Loyda B. Méndez ◽  
Andrea Ortíz-Rivera ◽  
Rosa I. Rodríguez-Cotto ◽  
Braulio Jiménez-Vélez
Keyword(s):  
Steady State ◽  
Inflammatory Mediators ◽  
Half Life ◽  
Transcriptional Control ◽  
Mrna Levels ◽  
Organic Extracts ◽  
Steady State Levels ◽  
Mrna Half Life ◽  
Cxcl8 Mrna ◽  
In Cells

Exposure to airborne particulate matter (PM) has been associated with the transcriptional up-regulation of pro-inflammatory mediators. However, the effect of PM on post-transcriptional regulation of pro-inflammatory mediators has not been fully explored. In this study, we examined the acute effect of organic extracts from urban PM, rural PM and diesel exhaust particles (DEP) on the post-transcriptional control of interleukin-6 (IL-6) and interleukin-8 (CXCL8) using a human bronchial epithelial cell line. Both PM and DEP extracts induced the release of IL-6 and CXCL8 after 24 h of exposure. Time-course experiments were conducted to examine changes in mRNA steady-state levels and half-lives. The steady-state levels of CXCL8 mRNA increase at 15 min on cells exposed to both PM and DEP extracts. Meanwhile only the urban extract induced significant increases of IL-6 mRNA levels at 15 min. Indirect measurements of IL-6 mRNA half-life showed a dramatic increase in cells exposed to the organic extracts. CXCL8 mRNA half-life increases in cells exposed to PM extracts and not DEP extract. Nuclear run-ons demonstrated that the urban PM and DEP extracts promoted an up-regulation in the transcription rate of CXCL8 at 15 min but not for IL-6. Urban and rural PM influences the post-transcriptional control of CXCL8.

scholarly journals Growth-Independent Regulation of CLN3mRNA Levels by Nutrients in Saccharomyces cerevisiae

1998 ◽  
Vol 180 (2) ◽  
pp. 225-230 ◽  
Author(s):  
Fereshteh Parviz ◽  
Warren Heideman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcriptional Control ◽  
Protein A ◽  
Nitrogen Sources ◽  
Mrna Levels ◽  
Rich Medium ◽  
Phase Growth ◽  
Protein Levels ◽  
In Cells

ABSTRACT Saccharomyces cerevisiae cells regulate progress through the G1 phase of the cell cycle in response to nutrients, moving quickly through G1 in rich medium and slowly in poor medium. Recent work has shown that the levels of Cln3 protein, a G1 cyclin, are low in cells growing in poor medium and high in cells growing rapidly in rich medium, consistent with the previously recognized role of Cln3 in promoting passage through Start. Cln3 protein levels appear to be regulated both transcriptionally and posttranscriptionally. We have worked to define the nutrient signals that regulate CLN3 mRNA levels. We find that CLN3 mRNA levels are high during log-phase growth in glucose medium, low in postdiauxic cells growing on ethanol, and slightly lower still in cells in stationary phase. CLN3mRNA levels are induced by glucose in a process that involves transcriptional control, requires metabolism of the glucose, and is independent of the Ras-cyclic AMP pathway. CLN3 mRNA levels are also positively regulated by nitrogen sources, but phosphorus and sulfur limitation do not affect CLN3 message levels.

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