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PubMed2005

The Rhizobium etli bioMNY operon is involved in biotin transport.

Because Rhizobium etli CE3 is normally dependent on an external source of biotin and lacks orthodox biotin biosynthesis genes, we undertook an analysis of biotin uptake in this organism. By complementation of a Sinorhizobium meliloti bioM mutant we isolated an R. etli chromosomal region encoding homologs of the S. meliloti bioMNB genes, whose products have been implicated in intracellular biotin retention in that organism. Disruption of the R. etli bioM resulted in a mutant which took up biotin at a lower rate and accumulated significantly less biotin than the wild type. As in S. meliloti, the R. etli bioMN gene-products resemble the ATPase and permease components, respectively, of an ABC-type transporter. The bioB gene product is in fact similar to members of the BioY family, which has been postulated to function in biotin transport, and we refer to this gene as bioY. An R. etli bioY mutant exhibited lower biotin uptake than the wild-type, providing the first experimental evidence for a role of BioY in biotin transport. We show that the bioMNY operon is transcriptionally repressed by biotin. An analysis of the competitiveness of the wild-type strain versus the bioM mutant showed that the mutant had a diminished capacity to form nodules on bean plants.

Adenosine Triphosphatases↗
PubMed1969

Regulation of synthesis of glutamate dehydrogenase and glutamine synthetase in micro-organisms.

1. Aspergillus nidulans, Neurospora crassa and Escherichia coli were grown on media containing a range of concentrations of nitrate, or ammonia, or urea, or l-glutamate, or l-glutamine as the sole source of nitrogen and the glutamate dehydrogenate and glutamine synthetase of the cells measured. 2. Aspergillus, Neurospora and Escherichia coli cells, grown on l-glutamate or on high concentrations of ammonia or on high concentrations of urea, possessed low glutamate dehydrogenase activity compared with cells grown on other nitrogen sources. 3. Aspergillus, Neurospora and Escherichia coli cells grown on l-glutamate possessed high glutamine synthetase activity compared with cells grown on other nitrogen sources. 4. The hypothesis is proposed that in Aspergillus, Neurospora and Escherichia colil-glutamate represses the synthesis of glutamate dehydrogenase and l-glutamine represses the synthesis of glutamine synthetase. 5. A comparison of the glutamine-synthesizing activity and the gamma-glutamyltransferase activity of glutamine synthetase in Aspergillus and Neurospora gave no indication that these fungi produce different forms of glutamine synthetase when grown on ammonia or l-glutamate as nitrogen sources.

Ammonia↗
PubMed1977

Unstable mutations that relieve catabolite repression of tryptophanase synthesis by Escherichia coli.

From strains of Escherichia coli that carry deletions of the trp region, five different mutants were isolated that were capable of synthesizing tryptophanase at unusually high rates in conditions of severe catabolite repression. Notwithstanding the comparative insensitivity to catabolite repression, the rates of tryptophanase synthesis in the mutants were greatly diminished by the introduction of a defective gene for adenyl cyclase. Each of the mutants segregated variants of the parental type. The results of genetic analysis appear to be consistent with the mutants arose by duplication of the tryptophanase gene.

Adenylyl Cyclases↗
PubMed1984

Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression.

Strain SF22, a glutamine-requiring (Gln-) mutant of Bacillus subtilis SMY, is likely to have a mutation in the structural gene for glutamine synthetase, since this strain synthesized 22 to 55% as much glutamine synthetase antigen as did wild-type cells in a 10-min period but had less than 3% of wild-type glutamine synthetase enzymatic activity. The expression of several genes subject to glucose catabolite repression was altered in the Gln- mutant. The induced levels of alpha-glucosidase, histidase, and aconitase were 3.5- to 4-fold higher in SF22 cells than in wild-type cells grown in glucose-glutamine medium, and citrate synthase levels were 8-fold higher in the Gln- mutant than in wild-type cells. The relief of glucose catabolite repression in the Gln- mutant may result from poor utilization of glucose. Examination of the intracellular metabolite pools of cells grown in glucose-glutamine medium showed that the glucose-6-phosphate pool was 2.5-fold lower, the pyruvate pool was 4-fold lower, and the 2-ketoglutarate pool was 2.5-fold lower in the Gln- cells than they were in wild-type cells. Intracellular levels of glutamine were sixfold higher in the Gln- mutant than in wild-type cells. Measurements of enzymes involved in glutamine transport and utilization showed that the elevated pools of glutamine in the Gln- mutant resulted from a threefold increase in glutamine permease and a fivefold decrease in glutamate synthase. The pleiotropic effect of the gln-22 mutation on the expression of several genes suggests that either the glutamine synthetase protein or its enzymatic product, glutamine, is involved in the regulation of several metabolic pathways in B. subtilis.

Bacillus subtilis↗
PubMed1986

Molecular cloning of cis-acting regulatory alleles of the Bacillus subtilis amyR region by using gene conversion transformation.

Three cis-acting alleles (gra-10, gra-5, and amyR2) of the Bacillus subtilis amyR promoter locus each cause catabolite repression-resistance of amyE-encoded alpha-amylase synthesis. The gra-10, gra-5, and amyR2 alleles were transferred from the chromosomes of their respective hosts to a plasmid carrying the amyR1-amyE+ gene by the process of gene conversion which is carried out during transformation of competent B. subtilis by plasmid clones carrying homologous DNA. The cloned amyR promoter regions containing the gra-10 and gra-5 mutations were shown to confer catabolite repression-resistance in cis to the synthesis of chloramphenicol acetyltransferase encoded by the cat-86 indicator gene when subcloned into the promoter-probe plasmid pPL603B. Implications concerning both the regulation of amyR utilization and the process of gene conversion in B. subtilis are discussed.

Alleles↗
PubMed1994

Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo.

The product of the SNF1 gene is a protein kinase whose activity is essential for transcriptional activation of glucose repressed genes in Saccharomyces cerevisiae. We have cloned a mammalian AMP-activated protein kinase (AMPK) that is 46% identical to the deduced amino acid sequence of SNF1 (Carling, D., Aguan, K., Woods, A., Verhoeven, A.J.M., Beri, R., Brennan, C.H., Sidebottom, C., Davison, M.D., and Scott, J. (1994) J. Biol. Chem. 269, 11442-11448). Mammalian AMPK plays a major role in the control of lipid metabolism and phosphorylating, thereby inactivating both acetyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl-CoA reductase, key regulatory enzymes in the synthesis of fatty acids and cholesterol, respectively. We present evidence indicating that, in common with its mammalian homologue, SNF1 forms part of a protein kinase cascade. SNF1 is inactivated in vitro by treatment with protein phosphatase 2A and can be reactivated using a partially purified preparation of mammalian AMPK kinase. SNF1 undergoes a time-dependent increase in activity during growth in glucose-derepressing conditions, providing the first evidence that SNF1 activity is regulated by the level of available glucose. In wild-type yeast, but not in a snf1 deletion mutant, acetyl-CoA carboxylase shows a reciprocal change in activity compared with SNF1 under glucose derepressing conditions, indicating that SNF1 regulates acetyl-CoA carboxylase in vivo. These results suggest that, in addition to their structural similarity, the role of SNF1 and AMPK in the regulation of fatty acid synthesis has been highly conserved throughout evolution.

AMP-Activated Protein Kinases↗
PubMed1996

Mother cell-specific HO expression in budding yeast depends on the unconventional myosin myo4p and other cytoplasmic proteins.

Certain cell types give rise to progeny that adopt different patterns of gene expression in the absence of any differences in their environment. Cells of budding yeast give birth to mother and daughter cells that differ in that only mother cells express the HO endonuclease gene and thereby switch mating types. We describe the identification of five genes, called SHE1-SHE5, that encode cytoplasmic proteins required for mother-specific HO expression. She1p, which is identical to the minimyosin Myo4p, and She3p are not, however, mother-specific proteins. On the contrary, they accumulate in growing buds. She proteins might be required for the transport of factors that promote HO repression from the mother cell into its bud. In an accompanying paper, we show that SHE genes are needed for the accumulation in daughter nuclei of Ash1p, a repressor of HO.

Cell Cycle↗
PubMed1997

Bacterial degradation of natural rubber: a privilege of actinomycetes?

Using natural rubber latex as the sole source of carbon and energy 50 rubber-degrading bacteria were isolated. Out of those 50 isolates, 33 were identified as Streptomyces species and 8 as Micromonospora species. Screening of 1220 bacteria obtained from different culture collections revealed 46 additional rubber-degrading bacteria (Streptomyces 31 strains, Micromonospora 5, Actinoplanes 3, Nocardia 2, Dactylosporangium 1, Actinomadura 1, unidentified 3). All rubber-degrading isolates were identified as members of the actinomycetes, a large group of mycelium-forming Gram-positive bacteria. Interestingly no Gram-negative bacterium could be isolated. In most strains expression of extracellular rubber-degrading enzymes was repressed by glucose and/or succinate. The reduction of the average molecular mass of solution-cast films of natural rubber from 640000 to 25000 in liquid culture upon bacterial growth indicates the participation of an endo-cleavage mechanism of degradation.

Actinomycetales↗
PubMed1999

Down-regulation of the expression of PKC1 and SRB1/PSA1/VIG9, two genes involved in cell wall integrity in Saccharomyces cerevisiae, causes flocculation.

The cell wall integrity determinants PKC1 and SRB1/PSA1/VIG9 of Saccharomyces cerevisiae were expressed under the control of the tightly regulated promoter pMET3. Substitution of the cell-cycle-regulated SRB1/PSA1 native promoter with pMET3 led to faster cell growth, larger cell volumes, and a twofold reduction of the steady-state SRB1/PSA1 mRNA level. In addition, the new pattern of expression of SRB1/PSA1 resulted in a dominant flocculation phenotype at all phases of batch growth. By contrast, expression of PKC1 from pMET3 increased the flocculation capacity of cells only at stationary phase. Methionine-mediated repression of either PSA1/SRB1 or PKC1 resulted in enhanced cell clumping. Cells in which both these genes had been replaced with their respective pMET3-regulated cassettes were highly flocculent under both expression and repression conditions. These results suggest that greater exposure of flocculin on the cell surface, caused by either cell wall distortion (through depletion of Pkc1p) or aberrant regulation of mannosylation (through constitutive production of Srb1p), results in an increased flocculation ability.

Cell Wall↗
PubMed1994

Catabolite repression of the Bacillus subtilis hut operon requires a cis-acting site located downstream of the transcription initiation site.

Expression of the Bacillus subtilis hut operon is subject to regulation by catabolite repression. A set of hut-lacZ transcriptional fusions was constructed and used to identify two cis-acting sites involved in catabolite repression. The hutOCR1 operator site lies immediately downstream of the hut promoter and weakly regulates hut expression in response to catabolite repression. The downstream hutOCR2 operator site lies within the hutP gene, between positions +203 and +216, and is required for wild-type levels of catabolite repression. Both the hutOCR1 and hutOCR2 operators have sequence similarity to the sites which mediate catabolite repression of several other B. subtilis genes. Two mutations which relieve catabolite repression of hut expression were found to alter the nucleotide sequence of the hutOCR2 operator. Catabolite repression of hut expression was partially relieved in strains containing the ccpA mutation but not in strains containing either the pai or hpr mutation.

Aldose-Ketose Isomerases↗
PubMed1980

Metabolite gene regulation of the L-arabinose operon in Escherichia coli with indoleacetic acid and other indole derivatives.

The ability of indole derivatives to facilitate RNA polymerase transcription of the L-arabinose operon in Escherichia coli was shown to require the catabolite activator protein (CAP) as well as the araC gene product. Adenosine 3',5'-monophosphate (cAMP) was not obligatory for araBAD transcription when the cells were grown in the presence of 1 mM indole-3-acetic acid or in the presence of indole-3-acetamide, indole-3-propionic acid, indole-3-butyric acid, or 5-hydroxyindole-3-acetic acid. However, these indole derivatives were unable to circumvent the cAMP requirement for the induction of the lactose and the maltose operons. Catabolic repression occurred when glucose was added to cells grown in the presence of L-arabinose and 1 mM indoleacetic acid or 1 mM cAMP. This effect was reversed at higher concentrations of indoleacetic acid or cAMP. The induction and the catabolite repression phenomena were quantitated by measuring the differential rate of synthesis of L-arabinose isomerase (the araA gene product). These results indicated that indole metabolites from various living systems may regulate gene expression and may be involved in "metabolite gene regulation."

Arabinose↗
PubMed1988

Regulation of manganese superoxide dismutase in Saccharomyces cerevisiae. The role of respiratory chain activity.

The importance of respiratory chain activity in the induction of manganese superoxide dismutase biosynthesis was examined in the yeast Saccharomyces cerevisiae by immunological measurement of the level of manganese superoxide dismutase and comparison with copper/zinc superoxide dismutase and two subunits of respiratory chain proteins, cytochrome c1 and core 2, under conditions of growth in which respiratory chain activity was varied. Oxygen consumption by the yeast was also monitored during growth. These comparative studies indicated that under normoxic conditions, glucose repression of the respiratory chain subunits resulted in a parallel repression of the level of manganese superoxide dismutase protein. The increase in the protein levels of manganese superoxide dismutase and core 2 protein under derepressing growth conditions reflected an increase in the level of the mRNA for each protein; thus regulation is, at least in part, at the level of transcription. The following observations support the conclusion that under normoxic conditions manganese superoxide dismutase biosynthesis is primarily regulated by the same means as the respiratory chain components; that is, by glucose (catabolite) repression rather than by oxygen metabolites. 1) When yeast cells were transferred from repressing to derepressing growth conditions in normoxia, manganese superoxide dismutase biosynthesis increased at a rate parallel to that of core 2, and occurred approximately 5 h in advance of increased oxygen consumption by the yeast. 2) When an important site of mitochondrial superoxide radical generation, the cytochrome bc1 complex, was inactivated by deletion of the gene coding for one of its subunits, the level of manganese superoxide dismutase protein was not changed in the mutant compared with the parental strain. However, regulation of manganese superoxide dismutase can be separated from regulation of the respiratory chain proteins in certain instances. During the transition from the logarithmic growth phase to the stationary phase in non-fermentable carbon sources, the level of manganese superoxide dismutase decreased by approximately 50%, whereas the levels of cytochrome c1 and core 2 remained unchanged. Furthermore, yeast grown in hyperoxia of 70-80% oxygen utilizing either repressing or depressing carbon sources, contained significantly higher levels of manganese superoxide dismutase and copper/zinc superoxide dismutase compared to yeast grown in normoxia, whereas the levels of respiratory chain proteins were not affected by hyperoxia.(ABSTRACT TRUNCATED AT 400 WORDS)

Electron Transport Complex III↗
PubMed1972

De novo biosynthesis of nicotinamide adenine dinucleotide in Escherichia coli: excretion of quinolinic acid by mutants lacking quinolinate phosphoribosyl transferase.

The excretion of quinolinic acid was studied in growing and resting cells of Escherichia coli K-12 nadC(13). Under optimal conditions, this organism could synthesize quinolinic acid in several-fold excess of the amount which would be required for normal growth. The excretion of quinolinic acid was controlled by the concentration of nicotinamide adenine dinucleotide (NAD) precursors available to the organism either during growth or during incubation in dense cell suspensions. These observations suggest that biosynthesis of NAD de novo is regulated by both repression and feedback inhibition. Analogues of niacin which inhibit bacterial growth also inhibited and repressed the synthesis (excretion) of quinolinic acid. The pH optimum for quinolinic acid excretion agreed favorably with the optimum observed for its synthesis in vitro. The rate of quinolinic acid excretion was strongly influenced by the concentration of ribose or glycerol in the medium.

Amino Acids↗
PubMed1977

[Repression and derepression of lactate dehydrogenase loci during mouse development].

The ultramicroelectrophoretic method was applied to the study of the lactic dehydrogenase (LDH) spectrum alterations during the developmental phases of mice: ovulated ova--zygote--blastocyte--embryo--oocyte--ovulated ova. Only H-subunits were found in the embryo cells before the 5th day of development. After this M-subunits appeared indicating derepression of LDH-A locus. On the 8th day of the embryonal development deres pression of the LDH-B locus was observed to disappear during the oogenesis, being the result of progressive repression of locus LDH-A. Dictiotena of meios prophase is characterised by active H-subunit synthesis and a gradual decrease of the M-subunit synthesis. During the whole dictiotena phase the LDH-spectrum of the follicular cells was of the M-type.

Animals↗
PubMed2002

Synthesis of alpha-amylase by Aspergillus oryzae in solid-state fermentation.

Spent Brewing Grains (SBG) was evaluated for its efficacy to be used as sole carbon source for the synthesis of alpha-amylase in solid-state fermentation using a fungal strain of Aspergillus oryzae NRRL 6270. Enzyme production was superior when the culture grew on mesophilic temperatures and best yields were at 25 degrees C. At 30 degrees C, yields were almost comparable. Maximum production of alpha-amylase [6870 U/g dry substrate (gds)] was obtained when SSF was carried out at 30 degrees C for 96 h using SBG medium, which had initial moisture of 70% and was inoculated using a spore suspension containing 1 x 10(7) spores/ml. Supplementation of SBG with external carbon sources such as mono-, di and polysaccharides caused repression in enzyme synthesis by the fungal culture.

Aspergillus oryzae↗
PubMed1978

The activity of ant product of the Salmonella phage P22 against the closely related but heteroimmune phage L.

P22 mutants defective in the early gene 24 are complemented by phage L in mixed infection. P22 12- and P22 23- mutants are not complemented by phage L. Gene function 24 of an L prophage is turned on by a superinfecting P22 24- mutant and complements the missing function of the defective P22 phage. Since this transactivation of prophage gene 24 depends on a functional gene ant in the superinfecting P22 mutant, it indicates derepression for leftward directed gene expression in prophage L. On the contrary neither the rightward directed expression of gene 12 nor of gene 23 in prophage L. can be turned on by superinfecting P22 24- 12- or P22 24- 23- mutants (and also not by P22 12- and P22 23-) to a degree sufficient for complementation of simultaneously superinfecting L virB 12- or L virB 23- mutants. The failure to detect release of repression for rightward directed gene expression of prophage L corresponds to the earlier observation (Prell, 1975) that P22 superinfecting L lysogens cannot release replication inhibition for simultaneously infecting phage L. The results are discussed with respect to the mechanism underlying the different action of P22 antirepressor in L and in P22 lysogens.

DNA Replication↗
PubMed1990

A novel function of the transforming domain of E1a: repression of AP-1 activity.

Adenovirus E1a represses transcription of the collagenase gene via the phorbol ester-responsive element (collTRE). The mechanism involves inhibition of the trans-activating function of the transcription factor AP-1 without reduction of its synthesis and without any apparent change in DNA binding or composition. The ability of E1a to downmodulate AP-1 is a unique property among dominant oncogenes. This repression depends on conserved region 1, one of the transforming domains of E1a, indicating that it is an integral feature of adenovirus transformation.

Adenovirus Early Proteins↗