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PubMed1998

A region of the cellobiohydrolase I promoter from the filamentous fungus Trichoderma reesei mediates glucose repression in Saccharomyces cerevisiae, dependent on mitochondrial activity.

The upstream activating region that controls cellulose-induced expression of the glucose-repressible cellobiohydrolase I gene (UARcb1) of the filamentous fungus Trichoderma reesei is shown to mediate transcription and glucose repression of a reporter gene in Saccharomyces cerevisiae, a unicellular microorganism that lacks the genes required for the utilization of cellulose. Glucose-controlled transcription mediated by UARcb1 requires the products of the genes SNF1 and SSN6, a protein kinase and a repressor, respectively, that regulate glucose-repressible yeast genes. Previously, it has been shown that mitochondrial function is implicated in cellobiohydrolase I gene expression in T. reesei and this sensitivity to the metabolic state of the mitochondria was shown to be transcriptionally controlled by the 5'-flanking sequence of the cbh1 gene [Abrahão-Neto et al. (1995) Biochemistry 34, 10456-10462]. Remarkably, transcription of the reporter gene controlled by UARcb1 in S. cerevisiae also showed a requirement for active mitochondria, suggesting that a common mechanism involving mitochondrial activity controls glucose-repressible genes in both microorganisms.

5' Untranslated Regions↗
PubMed1995

Stabilised secondary structure at a ribosomal binding site enhances translational repression in E. coli.

The expression of the gene encoding Escherichia coli threonyl-tRNA synthetase is negatively autoregulated at the translational level. The negative feedback is due to the binding of the synthetase to an operator site on its own mRNA located upstream of the initiation codon. The present work describes the characterisation of operator mutants that have the rare property of enhancing repression. These mutations cause (1) a low basal level of expression, (2) a temperature-dependent expression, and (3) an increased capacity of the synthetase to repress its own expression at low temperature. Surprisingly, this enhancement of repression is not explained by an increase of affinity of the mutant operators for the enzyme but by the formation, at low temperature, of a few supplementary base-pairs between the ribosomal binding site and a normally single-stranded domain of the operator. Although this additional base-pairing only slightly inhibits ribosome binding in the absence of repressor, simple thermodynamic considerations indicate that this is sufficient to increase repression. This increase is explained by the competition between the ribosome and repressor for overlapping regions of the mRNA. When the ribosomal binding site is base-paired, the ribosome cannot bind while the repressor can, giving the repressor the advantage in the competition. Thus, the existence of an open versus base-paired equilibrium in a ribosomal binding site of a translational operator amplifies the magnitude of control. This molecular amplification device might be an essential component of translational control considering the low free repressor/ribosome ratio of the low affinity of translational repressors for their target operators.

Base Composition↗
PubMed1976

Structural limits of specificity of methylcholanthrene-repressible nitrosamine N-dealkylases. Inhibition by analog substrates.

The dealkylation of dimethyl-, diethyl- and dipropylnitrosamine by hepatic microsomes of Sprague-Dawley rats is repressed by pretreatment of the animals with 3-methylcholanthrene (MC), and this repression progressively decreases with the increase of alkyl chain length. In contrast to its effect on the demethylation of dimethylnitrosamine (DMN), in vivo phenobarbital induces rather than represses the deethylation of diethylnitrosamine. The rates of demethylation of the DMN analog substrates (dimethylformamide, dimethylacetamide, dimethylpropionamide, and dimethylbutyramide), although low as compared to DMN, increase with the acyl chain length. These analogs are potent in vitro inhibitors of Dmn demethylation when used in combination with DMN as substrates, and the inhibition decreases with the length of the acyl chain. Dimethylaminoacetone, which corresponds to the insertion of a CH2 group between the N atom and the carbonyl group in dimethylacetamide, is not an in vitro inhibitor of DMN demethylation; the demethylation rates are additive when theis compound is used as substrate in combination with DMN. The rate of demethylation of dimethylaminoacetone is substantially higher than the rates of the dimethylacylamides, and is significantly repressed by MC-pretreatment. The rate of demethylation of methylphenylnitrosamine is not influenced by MC-pretreatment; the compound is, however, a potent inhibitor of demethylation when used as substrate in combination with DMN. The demethylation rates of 1,1-dimethylhydrazine (the reduction product of DMN) and dimethylaniline are not influenced by MC-pretreatment; neither do they affect the overall rate of demethylation when used as substrate in combination with DMN.

Animals↗
PubMed1983

Catabolite repression and nitrogen control of allantoin-degrading enzymes in Pseudomonas aeruginosa.

The formation of the allantoin-degrading enzymes allantoinase, allantoicase and ureidoglycolase in Pseudomonas aeruginosa was found to be regulated by induction, catabolite repression and nitrogen control. Induction was observed when urate, allantoin or allantoate were included in the growth medium, but not with ureidoglycolate. Tricarboxylic acid cycle intermediates exerted catabolite repression of the synthesis of the three enzymes, while pyruvate and glucose caused less repression. The operation of a nitrogen control mechanism in the regulation of the allantoin-degrading enzymes could be demonstrated with glutamine synthetase-negative mutants, which showed elevated synthesis and escape from catabolite repression when growth was limited for glutamine.

Allantoin↗
PubMed1986

Molecular events associated with glucose repression of invertase in Saccharomyces cerevisiae.

When S. cerevisiae growing in the presence of glucose (repressive condition) was shifted to higher temperatures, invertase was secreted. This secretion required protein synthesis, but was independent of RNA formation (Mormeneo & Sentandreu 1982). In addition accumulation of invertasespecific messenger RNA occurred in the absence of protein synthesis but was expressed only after synthesis of protein. Invertase mRNA was continuously synthesized under repressive conditions and the levels of this mRNA were regulated by the presence of glucose. The hexose regulated the concentration of this mRNA at the level of transcription and/or by sensitization of this messenger RNA. The expression of the invertase mRNA present in the cells under repressive conditions was also regulated by glucose at the level of translation and/or secretion. As a result of these processes, under repressive conditions invertase is eliminated before secretion takes place.

Culture Media↗
PubMed1976

[Relations between catabolite repression and sporulation in Bacillus subtilis (author's transl)].

Acetoin dehydrogenase can be catabolite repressed by numerous sources of carbon. The following results point out that the catabolite repression of this enzyme and the inhibition of sporulation are mediated by the same mechanism: 1. Mutants, able to synthesize acetoin dehydrogenase in the presence of glucose, sporulate in glucose medium at a higher rate than the standard strain. 2. The catabolite repressing effect of a compound and its ability to inhibit sporulation are in a direct relation to each other. 3. The limitation of inorganic phosphate in the growth medium, which is known to favour sporulation, counteracts the catabolite repressing effect of glucose.

Acetoin Dehydrogenase↗
PubMed1985

Repression and inhibition of cephalosporin synthetases in Streptomyces clavuligerus by inorganic phosphate.

Cephalosporin production by growing cells of Streptomyces clavuligerus was reduced by 100 mM inorganic phosphate. Resting cell production was repressed by prior growth in high phosphate and inhibited by phosphate. The cell-free activity of desacetoxycephalosporin C synthetase (ring expansion activity) was repressed by prior growth in high phosphate and inhibited by phosphate. Isopenicillin N synthetase (cyclase) was inhibited but not repressed. Penicillin epimerase was neither inhibited nor repressed by phosphate.

Cephalosporins↗
PubMed1975

Effect of cyclic AMP on catabolite repressed bacterial sporogenesis of an anaerobe.

The sporulation of a high frequency sporogenic mutant of Clostridium botulinum was reduced to less than 30% in a medium containing 270 mM glucose. The repression was reversed from 30 to greater than 80% sporulation by the addition of 10(-5) or 10(-4) M cyclic 3',5'-adenosine monophosphate (cAMP) or monobutyrul cyclic AMP (B-cAMP). No difference was observed in amount of growth with the addition of either the cAMP or B-cAMP. Glucose consumption was enhanced by the addition of either of the cyclic nucleotides and corresponding changes in pH were observed. The catabolite repression by glucose was reversed by ATP or ADP. Except for GTP, guanine nucleotides were not effective. The intracellular cyclic AMP levels were high in vegetative, sporulating and derepressed cells, but low in glucose-repressed cells. The findings suggest that the sporulation of the anaerobe was sensitive to catabolite repression which was specifically reversed by cyclic AMP.

Adenine Nucleotides↗
PubMed1978

Effect of the mouse mutants testicular feminization and sex reversal on hormone-mediated induction and repression of enzymes.

The mouse mutants testicular feminization and sex reversal have been used to investigate hormone-mediated induction and repression of enzymes. Tfm/Y animals were already known to be androgen insensitive, rendering the androgen-inducible enzymes ADH and beta-glucuronidase noninducible because of an inherited deficiency of a cytosol androgen-receptor complex. The animals display female secondary sexual characteristics. Sxr/+,XX animals display male primary and secondary sexual characteristics with small testes. We demonstrate (1) that the Tfm mutation is pleiotropic, preventing repression of an androgen-repressible enzyme (ornithine aminotransferase) as well as induction of androgen-inducible enzymes, (2) that an estrogen-inducible enzyme (histidine decarboxylase) is not affected by the Tfm mutation, and (3) that Sxr/+,XX animals produce enough androgen for malelike activities of androgen-sensitive enzymes. It was also discovered that histidine decarboxylase repressed by androgen in normal animals, rather than being unaffected by it in Tfm/Y animals, is in fact induced. This unexpected phenomenon is discussed and an explanation is suggested for it.

Alcohol Oxidoreductases↗
PubMed1975

Penicillinamidohydrolase in Escherichia coli. III. Catabolite repression, diauxie, effect of cAMP and nature of the enzyme induction.

Synthesis of penicillinamidohydrolase (penicillin acylase, EC 3.5.1.11) in Escherichia coli is subjected to the absolute catabolite repression by glucose and partial repression by acetate. Both types of catabolite repression of synthesis of the enzyme in Escherichia coli are substantially influenced by cyclic 3',5'-adenosinemonophosphate (cAMP). Growth diauxie in a mixed medium containing glucose and phenylacetic acid serving as carbon and energy sources is overcome by cAMP. cAMP does not influence the basal rate of the enzyme synthesis (without the inducer). Derepression of synthesis of penicillinamidohydrolase by cAMP in a medium with glucose and inducer (phenylacetic acid) is associated with utilization of the inducer, due probably to derepression of other enzymes responsible for degradation of phenylacetic acid. Lactate can serve as a "catabolically neutral" source of carbon suitable for the maximum production of penicillinamidohydrolase. The gratuitous induction of the enzyme synthesis in a medium with lactate as the carbon and energy source and with phenylacetic acid is not influenced by cAMP; however, cAMP overcomes completely the absolute catabolite repression of the enzyme synthesis by glucose.

Acetates↗
PubMed1981

Catabolite repression of different inducible enzymes in Escherichia coli and the effect of cAMP.

Simultaneous induction of two enzymes sensitive to catabolite repression does not lead to an additive decrease of the specific activity of the two. Exogenously added cAMP increases the specific activity of catabolically repressed enzymes, irrespective of whether the enzyme is induced separately or simultaneously with another enzyme. In the presence of 12 different substrates metabolized by inducible enzymes glucose does not bring about catabolite repression. Synthesis of cAMP is identical with that occurring under conditions when glucose brings about catabolite repression.

Cyclic AMP↗
PubMed1978

Catabolite repression of isocitrate lyase in methylamine-grown Pseudomonas MA. Effect of carbon and nitrogen sources.

The synthesis of the C1-type isocitrate lyase found during growth of Pseudomonas MA on methylamine was investigated. It was shown that this enzyme is subject to catabolite repression by preferred carbon sources, e.g., succinate, and by ammonia. The carbon repression can be overcome by cyclic AMP, which was shown to be acting at the transcriptional level. Repression by ammonia is overcome during growth with methylamine as sole nitrogen, but not carbon, source. Uptake experiments showed that the uptake of methylamine from the medium was prevented by ammonia in the presence, but not in the absence, of an alternative carbon source. Measurement of cyclic AMP levels in cells grown on methylamine and on succinate, glycerol, glucose and acetate as carbon sources (with ammonium chloride as nitrogen source) revealed that methylamine-grown cells have the lowest cyclic AMP level despite having the highest C1-type isocitrate lyase activity. Cells grown on acetate with methylamine as sole nitrogen source possess both C1-type and C2-type isocitrate lyase. The results indicate that the synthesis of C1-isocitrate lyase is under control by repression-derepression involving a specific inducer, cyclic AMP, and an effector whose action is related to the nitrogen supply of the cell.

Ammonia↗
PubMed1982

Purification and identification of inactive forms of repressible and constitutive acid phosphatase in yeast.

Acid phosphatase (EC 3.1.3.2, orthophosphoric-monoester phosphohydrolase, (acid optimum) from the budding yeast Saccharomyces cerevisiae was purified from repressed and derepressed cells. Without Triton X-100 in the extraction buffer only the constitutive or repressible active enzyme eluted from a Sepharose CL-6B column, the last step of the purification procedure. When Triton X-100 was included in the extraction buffer, an additional protein peak eluted prior to the active acid phosphatase. The material from this new peak, a glycoprotein, had no acid phosphatase activity but cross-reacted with antibodies raised against repressible acid phosphate. The tryptic fingerprints of the inactive proteins are very similar to the ones of the corresponding active enzymes. We conclude that this new glycoprotein represents an inactive form of repressible and constitutive acid phosphatase. The fact that inactive acid phosphatase can be recovered only in the presence of Triton X-100 indicates that it is membrane-bound.

Acid Phosphatase↗
PubMed2006

Marked sexual dimorphism of lacrimal gland peroxidase in hamster: repression by androgens and estrogens.

Peroxidase secreted in tears by the lacrimal glands is a marker of secretory activity of these glands and is believed to have an antimicrobial function. We report for the first time a marked sex difference in lacrimal gland (LG) peroxidase in hamsters ( approximately 3.4-fold higher activity in females), which is due to an unusual repression by physiological levels of androgens in males. LG peroxidase activity was markedly induced in a time-dependent manner after gonadectomy in males and also females ( approximately 8- and 2-fold, respectively) and was strongly repressed by androgen treatment in a dose- and time-dependent manner. Estrogen treatment of gonadectomized hamsters could also repress LG peroxidase but not below female levels. These repressions by androgens and estrogens were significantly prevented upon co-treatment with their respective receptor antagonists. Western blotting showed that differences in LG peroxidase specific activity, in different sex hormonal states and treatments were due to changes in the levels of peroxidase protein in LG. A tear peroxidase with a clear sex difference suggests that it might also have other novel function(s) in hamster tears.

Androgens↗
PubMed2005

Retrieval inhibition of trauma-related words in women reporting repressed or recovered memories of childhood sexual abuse.

Several authors have argued that survivors of childhood sexual abuse (CSA) who report to have repressed their traumatic memories are more skilled in forgetting emotional stimuli than survivors who have always remembered the abuse. The current experiment employed a list-wise directed forgetting task to investigate whether women reporting repressed (n = 16) or recovered (n = 23) memories of CSA are better at forgetting disturbing material, relative to women reporting having always remembered their abuse (n = 55) or reporting no history of abuse (n = 20). We found no support for the hypothesis that women reporting repressed or recovered memories of CSA are especially versed in inhibiting retrieval of trauma-related words. Additional analyses revealed that participants characterized by a repressive coping style did not display a superior retrieval inhibition mechanism for negative material.

Adult↗
PubMed2005

NSPc1, a mainly nuclear localized protein of novel PcG family members, has a transcription repression activity related to its PKC phosphorylation site at S183.

Nervous system polycomb 1 (NSPc1) shares high homology with vertebrate PcG proteins Mel-18 and Bmi-1. The mRNA of NSPc1 is highly expressed in the developmental nervous system [Mech. Dev. 102 (2001) 219-222]. However, the functional characterization of NSPc1 protein is not clear. In the present study, using Western blotting technique, we aimed to describe the distributions of NSPc1 protein in rat tissues and cell lines. The subcellular localization of NSPc1 was examined in HeLa and SH-SY5Ycell lines, and its transcriptional repression activity was examined in COS-7 cell line. We found that the NSPc1 protein was localized mainly in the nucleus. NSPc1 remarkably repressed the transcription. Most interestingly, both the C-terminal of NSPc1 and two phosphorylation sites in the C-terminal, especially the PKC phosphorylation site at S183, were important in mediating transcription repression. Taken together, results from our study suggest that NSPc1, as a typical PcG family member, has powerful transcriptional repression ability, which may be related to the PKC signaling pathway.

Animals↗
PubMed2005

Sleep paralysis in adults reporting repressed, recovered, or continuous memories of childhood sexual abuse.

Sleep paralysis typically occurs as individuals awaken from rapid eye movement sleep before motor paralysis wanes. Many episodes are accompanied by tactile and visual hallucinations, often of threatening intruders in the bedroom. Pendergrast [Victims of Memory: Incest Accusations and Shattered Lives, HarperCollins, London, 1996] proposed that individuals who report repressed or recovered memories of childhood sexual abuse (CSA) may misinterpret episodes of sleep paralysis as reemerging fragments of dissociated ("repressed") memories of CSA. To investigate this issue, we administered a sleep paralysis questionnaire to people reporting either repressed (n = 18), recovered (n = 14), or continuous (n = 36) memories of CSA, or to a control group reporting no history of CSA (n = 16). The prevalence of sleep paralysis was: repressed memory group (44%), recovered memory group (43%), continuous memory group (47%), and control group (13%). Among the six individuals in the recovered memory group who had experienced sleep paralysis, one interpreted it as related to sexual abuse (i.e., a rate of 17%). All other participants who had reported sleep paralysis embraced other interpretations (e.g., saw a ghost). Dissociation and depressive symptoms were more common among those who had experienced sleep paralysis than among those who denied having experienced it.

Adult↗
PubMed2026

Acetic acid-induced translational repression involves eIF2B body formation and Ded1 sequestration into stress granules in yeast.

Elucidating the physiological impact of acetic acid stress and the corresponding yeast responses is essential for advancing fundamental biology and improving industrial alcoholic fermentation. Despite numerous genome-wide studies, information on the effects of acetic acid stress on yeast translational regulation remains limited. We found that a sublethal concentration of acetic acid (35 mM, 0.2% v/v) causes translational repression, accompanied by the formation of eIF2B bodies and the phosphorylation of eIF2α, both of which are involved in the regulation of translation initiation. Acetic acid also caused the sequestration of Ded1, a DEAD-box RNA helicase crucial for translation initiation, into stress granules. Removal of acetic acid restored translational activity and the proper localization of eIF2B and Ded1, indicating the reversibility of acetic acid-induced translational repression. Furthermore, when yeast cells were pretreated with 0.05% acetic acid, translational repression under subsequent 0.2% acetic acid stress was attenuated in wild-type cells but not in hrk1Δ cells. This indicates that Hrk1, a Pma1 activator, is required to sufficiently enhance tolerance to acetic acid-induced translational repression. These findings provide novel insights into the physiological effects of acetic acid stress on translational activity and translation-related factors in yeast cells.

Saccharomyces cerevisiae↗