Sudden depletion of carbon source blocks translation, but not transcription, in the yeast <i>Saccharomyces cerevisiae</i>

Martínez‐Pastor, María Teresa; Estruch, Francisco

doi:10.1016/0014-5793(96)00683-7

Cited by 32 publications

(29 citation statements)

References 21 publications

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“…Overexpression of Phosphoglucomutase Reverts Inhibition of Protein Synthesis-Inhibition of protein synthesis at the initiation step has been show to occur after depletion of glucose or fructose (20,21). In a previous report (6) we have shown that lithium inhibits with high affinity phosphoglucomutase, an essential enzyme for galactose metabolism.…”

Section: Tif2 Confers Lithiummentioning

confidence: 94%

“…Lithium Versus Glucose Starvation-Lithium treatment in galactose-grown cells leads to inhibition of protein synthesis as has been shown for glucose starvation (20,21). In order to test if these two treatments lead to the dissociation of eIF4A from the preinitiation complexes, we have imposed glucose starvation in the absence of lithium by shifting cells to 0.05% glucose (Fig.…”

Section: Fig 2 Lithium Inhibits Initiation Of Protein Synthesis In mentioning

confidence: 98%

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The Initiation Factor eIF4A Is Involved in the Response to Lithium Stress in Saccharomyces cerevisiae

Montero-Lomelı́¹,

Morais

Figueiredo

et al. 2002

Journal of Biological Chemistry

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A gene, TIF2, was identified as corresponding to the translation initiation factor eIF4A and when overexpressed it confers lithium tolerance in galactose medium to Saccharomyces cerevisiae. Incubation of yeast with 6 mM LiCl in galactose medium leads to inhibition of [ 35 S]methionine incorporation. By polysome analysis we show that translation is inhibited by lithium at the initiation step, accumulating 80 S monosomes. We further show by immunoblot analysis that when cells are incubated with lithium eIF4A does not sediment with ribosomal subunits. Overexpression of TIF2 overcomes inhibition of protein synthesis and restores its sedimentation with the initiation complex. In vivo, eIF4A is induced by lithium stress. We have shown previously that lithium is highly toxic to yeast when grown in galactose medium mainly due to inhibition of phosphoglucomutase, an enzyme responsible for the entry of galactose into glycolysis. We show that conditions that revert inhibition of phosphoglucomutase also revert inhibition of protein synthesis. Interestingly, glucose starvation leads to loss of polysomes but not to dissociation of eIF4A from the preinitiation complexes. Overexpression of SIT4, a protein phosphatase related to the TOR kinase pathway, reverts inhibition of protein synthesis by lithium and association of eIF4A with the initiation complex.

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Section: Tif2 Confers Lithiummentioning

confidence: 94%

Section: Fig 2 Lithium Inhibits Initiation Of Protein Synthesis In mentioning

confidence: 98%

The Initiation Factor eIF4A Is Involved in the Response to Lithium Stress in Saccharomyces cerevisiae

Montero-Lomelı́¹,

Morais

Figueiredo

et al. 2002

Journal of Biological Chemistry

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“…The frequent mismatch between the kinetics of the expression of SUC2 and sucrose removal from the medium has at least two explanations. Either, another of the reported SUC genes 17,18 is of greater importance to sucrose hydrolysis or else invertase activity is primarily controlled posttranscriptionally 31,36,62 . Whatever the precise basis for the constitutive invertase phenotype manifested here, high invertase activity remains an important attribute of strains used in brewery fermentations in which wort fermentable carbohydrate content is commonly increased with high concentrations of sucrose 11,56 .…”

Section: (-7'977-32mentioning

confidence: 99%

Expression Patterns of Genes and Enzymes Involved in Sugar Catabolism in IndustrialSaccharomyces cerevisiaeStrains Displaying Novel Fermentation Characteristics

Meneses

Jiranek

2002

Journal of the Institute of Brewing

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The utilisation of maltose or sucrose by a selection of nine brewing, baking or laboratory strains of Saccharomyces cerevisiae was either repressible, constitutive or absent. Overall fermentation rate showed a good correlation with maximum specific maltose transport rate (R 2 = 0.79), but a poor correlation with maximum maltase activity (R 2 = 0.34), implying that transport rather than hydrolysis of maltose was a rate-limiting step determining fermentation performance. The genetic basis for differences seen between the strains in terms of fermentation kinetics was investigated. All strains were found to possess genomic sequences detectable with probes for the MAL11 (AGT1), MAL31 permease genes and the SUC2 invertase gene, however, the loci present and the pattern of expression of these and other MAL genes varied widely. From comparisons of sugar utilisation and gene expression patterns, constitutive maltose utilisation in strain NCYC 1681 was best explained by AGT1 expression. Such expression of AGT1 was not, however, mirrored by changes in the pattern of expression of the transcriptional activator(s) (MALx3). Patterns of sucrose utilisation were poorly predicted by the kinetics of SUC2 gene expression, indicating that other SUC loci may be of greater importance.

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“…There are three major pathways responsible for glucose-regulated gene expression in S. cerevisiae: the main glucose repression pathway, the cAMP-dependent protein kinase (cAPK) pathway, and the hexose transporter gene (HXT) induction pathway (Thevelein, 1994;Colombo et al, 1998;Gancedo, 1998;Carlson, 1999;Rolland et al, 2001; Figure 1B). Glucose deprivation also rapidly inhibits translation initiation (Martinez-Pastor and Estruch, 1996;Ashe et al, 2000). Ashe et al (2000) reported that several mutants affected in the glucose-sensing signal transduction pathways are resistant to the inhibitory effect of glucose removal on translation initiation.…”

Section: Introductionmentioning

confidence: 99%

Simultaneous yet Independent Regulation of Actin Cytoskeletal Organization and Translation Initiation by Glucose inSaccharomyces cerevisiae

Uesono

Ashe

Toh‐e

2004

MBoC

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Acute glucose deprivation rapidly but transiently depolarizes the actin cytoskeleton and inhibits translation initiation in Saccharomyces cerevisiae. Neither rapid actin depolarization nor translation inhibition upon glucose removal occurs in a reg1 disruptant, which is defective in glucose repression, or in the tpk1 w mutant, which has weak cAPK activity. In the absence of additional glucose, recovery of either actin polarization or translation initiation relies upon respiration, the Snf1p protein kinase, and the transcription factors Msn2p and Msn4p. The readdition of glucose to glucose-starved cells causes a rapid recovery of actin polarization as well as translation initiation without respiration. These results indicate that the simultaneous regulation of actin polarization and translation initiation is divided into three reactions: 1) rapid shutdown depending on Reg1p and cAPK after glucose removal, 2) slow adaptation depending on Snf1p and Msn2p/4p in the absence of glucose, and 3) rapid recovery upon readdition of glucose. On glucose removal, translation initiation is rapidly inhibited in a rom2 disruptant, which is defective in rapid actin depolarization, whereas rapid actin depolarization occurs in a pop2/caf1 disruptant, which is defective in rapid inhibition of translation initiation. Thus, translation initiation and actin polarization seem to be simultaneously but independently regulated by glucose deprivation. INTRODUCTIONThe actin cytoskeleton provides the structural basis for cell polarity in the yeast Saccharomyces cerevisiae and is organized primarily into two morphologically distinct structures: cortical patches and cables (Botstein et al., 1997). Cortical patches are discrete cytoskeletal bodies at the plasma membrane, whereas actin cables are long bundles of actin filaments that are oriented along the mother-bud axis. Both structures are polarized during the budding phase of the cell cycle. During early G1 phase, cortical patches and cables are randomly distributed. As a bud emerges, cortical patches cluster at the growing tip and cables extend from the mother cell into the bud. Near the end of bud growth, the patches and cables redistribute randomly, disrupting the asymmetric distribution of the actin cytoskeleton. At the end of mitosis, patches accumulate in and cables reorient toward the mother-bud neck in connection with cytokinesis and septum formation (Botstein et al., 1997).The actin cytoskeleton is also regulated in response to environmental stimuli. Mating pheromone causes polarization of the actin cytoskeleton toward the tip of the mating projection via the Cdc42p GTPase (Read et al., 1992;Leberer et al., 1997). In contrast, stresses such as osmotic shock, heat shock, and glucose starvation depolarize the actin cytoskeleton in budded cells as shown in Figure 1A (Novick et al., 1989;Chowdhury et al., 1992;Delley and Hall, 1999). In particular, the depolarization by heat or osmotic stress is known to be a rapid and transient reaction. A recent report has indicated that the rapid depol...

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Sudden depletion of carbon source blocks translation, but not transcription, in the yeast Saccharomyces cerevisiae

Cited by 32 publications

References 21 publications

The Initiation Factor eIF4A Is Involved in the Response to Lithium Stress in Saccharomyces cerevisiae

The Initiation Factor eIF4A Is Involved in the Response to Lithium Stress in Saccharomyces cerevisiae

Expression Patterns of Genes and Enzymes Involved in Sugar Catabolism in IndustrialSaccharomyces cerevisiaeStrains Displaying Novel Fermentation Characteristics

Simultaneous yet Independent Regulation of Actin Cytoskeletal Organization and Translation Initiation by Glucose inSaccharomyces cerevisiae

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