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PubMed1981

Association of Formation and Release of Cyclic AMP with Glucose Depletion and Onset of Chlorophyll Synthesis in Poterioochromonas malhamensis.

Depletion of glucose from the culture medium by Poterioochromonas malhamensis results in cessation of growth and accumulation of cyclic adenosine 3':5'-monophosphate (cAMP), followed by formation of chlorophyll and an increase in extracellular cAMP. Readdition of glucose to the culture medium causes P. malhamensis to release its intracellular cAMP into the medium. These results suggest that formation of the photosynthetic apparatus in P. malhamensis may be repressed by glucose, and that high cAMP conveys the regulatory information that the glucose supply is inadequate. This pattern is reminiscent of cAMP-mediated escape from catabolite repression in bacteria.

Journal Article↗
PubMed1980

[Study of a pts-gene-linked pleiotropic mutation influencing expression of catabolyte-sensitive genes of Escherichia coli K-12].

Properties of the pleiotropic mutation pts17 are described. This mutation is liked to pts1 gene, which specifies the synthesis of the enzyme I of phosphoenolpyruvate-dependent phosphotransferase system (PTS) in Escherichia coli K-12. Genetic analysis has shown that pts17 mutation is located between purC and pts1 markers and that the wild type allele pts17+ has transdominant character over the mutant allele pts17. The mutant strain J6217, isogenic to parent J62, shows normal growth properties in the minimal salt media with a number of carbohydrates used as a single carbon source. The pts17 mutations does not affect the enzyme I activity, but significantly suppresses the total PTS activity in the bacterial cell extracts. The intact mutant cells reveal the enhanced rate of accumulation and phosphorylation of alpha-methylglucoside. The pts17 bacteria show 3-fold enhanced phosphohydrolase activity with glucose-6-phosphate as substrate. It is established that pts17 mutation decreases the differential rate of the L-tryptophanase synthesis and makes the process of unductions resistant to glucose catabolite repression. It is suggested that this mutation affects the activity of the PTS factor III. One can suppose that the latter mediates the influence of ptsI and ptsH mutations upon the expression of catabolite-sensitive operons in E. coli.

Chromosome Mapping↗
PubMed1988

Differences in the regulation of aldehyde dehydrogenase genes in Aspergillus niger and Aspergillus nidulans.

In order to study mechanisms of gene regulation in A. niger, and to compare these to similar systems in A. nidulans, a gene encoding an aldehyde dehydrogenase enzyme has been cloned. In wild-type strains of A. niger the gene shows expression which is regulated by induction and repression. Levels of induction by various compounds and the extent of repression under various growth conditions differs from that seen for the A. nidulans aldA gene. Unlike the A. nidulans aldA gene, the A. niger gene has both carbon catabolite repressible and nonrepressible induction mechanisms. Studies of heterologous expression of the A. niger gene in A. nidulans have shown that its expression is regulated by the alcR gene product of A. nidulans.

Aldehyde Dehydrogenase↗
PubMed1999

Analysis of a ptsH homologue from Streptomyces coelicolor A3(2).

A ptsH homologue of Streptomyces coelicolor A3(2) was identified in the emerging genome sequence, cloned in Escherichia coli and the S. coelicolor HPr over-produced and purified. The protein was phosphorylated in vitro in a phosphoenolpyruvate (PEP)-dependent manner by purified enzyme I (EI) from Bacillus subtilis, and much less efficiently in an ATP-dependent manner by purified HPr kinase, also from B. subtilis. There was no indication of ATP-dependent phosphorylation of the purified protein by cell extracts of either S. coelicolor or Streptomyces lividans. Deletion of the ptsH homologue from the S. coelicolor and S. lividans chromosomes had no effect on growth when fructose was supplied as sole carbon source, and in S. coelicolor it had no effect on glucose repression of agarase and galactokinase synthesis, suggesting that the HPr encoded by this gene does not play an essential role in fructose transport nor a general role in carbon catabolite repression.

Adenosine Triphosphate↗
PubMed1995

Nucleotide sequence, transcriptional analysis, and glucose regulation of the phenoxazinone synthase gene (phsA) from Streptomyces antibioticus.

The nucleotide sequence of a 2.3-kb SphI fragment containing the structural gene (phsA) for phenoxazinone synthase (PHS) of Streptomyces antibioticus was determined. The sequence was found to contain an open reading frame (ORF) with a G+C content of 71.5% oriented in the direction of transcription that was confirmed by primer extension. The ORF encodes a protein with an M(r) of 70,223 consisting of 642 amino acids and is preceded by a potential ribosome-binding site. The codon usage pattern is in agreement with the general pattern for streptomycete genes, with a 92.5 mol% G+C content in the third position. The N-terminal sequence of the mature PHS subunit corresponds exactly to that predicted from the nucleotide sequence. Neither ATG nor GTG initiator codons were identified for the protein. However, a TTG codon was located near the amino terminus of the mature protein and is a good candidate for the initiator codon. The transcriptional start point of phsA was located 36 bp upstream of the start codon by primer extension. The -10 region of the putative promoter showed some similarity to the consensus sequence for the major class of prokaryotic promoters, but the -35 region was less similar. Comparison of the primary amino acid sequence of PHS of S. antibioticus with other amino acid sequences indicated that PHS is a blue copper protein with copper binding domains in the N-terminal and C-terminal regions of the polypeptide chain. A BsrBI fragment containing the promoter region of phsA and a portion of the ORF was shown to promote xylE expression when cloned in the streptomycete promoter probe vector pIJ2843. This phsA promoter-dependent xylE expression could be repressed by glucose in S. antibioticus when the organism was grown on glucose or galactose plus glucose. Thus, the cloned promoter region appears to contain the sequences responsible for catabolite repression of PHS production.

Amino Acid Sequence↗
PubMed1999

The bvr locus of Listeria monocytogenes mediates virulence gene repression by beta-glucosides.

The beta-glucoside cellobiose has been reported to specifically repress the PrfA-dependent virulence genes hly and plcA in Listeria monocytogenes NCTC 7973. This led to the hypothesis that beta-glucosides, sugars of plant origin, may act as signal molecules, preventing the expression of virulence genes if L. monocytogenes is living in its natural habitat (soil). In three other laboratory strains (EGD, L028, and 10403S), however, the effect of cellobiose was not unique, and all fermentable carbohydrates repressed hly. This suggested that the downregulation of virulence genes by beta-glucosides is not a specific phenomenon but, rather, an aspect of a global regulatory mechanism of catabolite repression (CR). We assessed the effect of carbohydrates on virulence gene expression in a panel of wild-type isolates of L. monocytogenes by using the PrfA-dependent phospholipase C gene plcB as a reporter. Utilization of any fermentable sugar caused plcB repression in wild-type L. monocytogenes. However, an EGD variant was identified in which, as in NCTC 7973, plcB was only repressed by beta-glucosides. Thus, the regulation of L. monocytogenes virulence genes by sugars appears to be mediated by two separate mechanisms, one presumably involving a CR pathway and another specifically responding to beta-glucosides. We have identified in L. monocytogenes a 4-kb operon, bvrABC, encoding an antiterminator of the BglG family (bvrA), a beta-glucoside-specific enzyme II permease component of the phosphoenolpyruvate-sugar phosphotransferase system (bvrB), and a putative ADP-ribosylglycohydrolase (bvrC). Low-stringency Southern blots showed that this locus is absent from other Listeria spp. Transcription of bvrB was induced by cellobiose and salicin but not by arbutin. Disruption of the bvr operon by replacing part of bvrAB with an interposon abolished the repression by cellobiose and salicin but not that by arbutin. Our data indicate that the bvr locus encodes a beta-glucoside-specific sensor that mediates virulence gene repression upon detection of cellobiose and salicin. Bvr is the first sensory system found in L. monocytogenes that is involved in environmental regulation of virulence genes.

Bacterial Proteins↗
PubMed1982

Influence of the rho-15 temperature-sensitive (ts) mutation on the expression of the deo-operon in Escherichia coli.

In the rho-15 temperature-sensitive (ts) mutant deo-operon enzymes show no sensitivity to catabolite repression and are not derepressed under the influence of a constitutive regulatory mutation, cytR. These data suggest that intact Rho-protein along with CRP protein is necessary for a catabolite sensitive deo-operon promoter cytP to work. In addition, there are data suggesting that Rho-factor and CRP-protein interact with each other in regulation of the deo-operon. Thus, in studies of the effect of the rho-15 (ts) and crp mutations, maximum deo-enzyme levels have been found in the double rho-15 (ts) crp mutant, and therefore intact Rho-protein in the crp genome or intact CRP-protein on the rho-15 (ts) background seems to be an obstacle for the deoP promoter in the deo-operon. In rho-15 (ts) a relative increase has been observed in the enzyme activity for a distal purine nucleoside phosphorylase gene with respect to a proximal thymidine phosphorylase gene. However in crp, the rho-15 (ts) mutation has no effect on the polarity gradient, that is on the background of impaired CRP protein Rho-factor does not seem to work as a transcription terminator within the operon.

Escherichia coli↗
PubMed1990

Two different mechanisms for urea action at the LAC and TNA operons in Escherichia coli.

Urea, at concentrations which do not interfere with bacterial growth, specifically inhibits the expression of catabolite sensitive operons. To search for the target and the mechanism of urea action we measured lactose (lac) and tryptophanase (tna) specific mRNA synthesis in vivo and in vitro. We show that urea acts by two different mechanisms at these two catabolite sensitive operons, resembling the manner in which catabolite repression regulates lac and tna. At the lac promoter, urea abolishes transcription initiation or blocks an early step in mRNA elongation without interfering with the binding of RNA polymerase and catabolite gene activator protein (CAP). At the tna promoter, urea does not abolish transcription initiation but could interfere with tnaC translation.

Cyclic AMP Receptor Protein↗
PubMed1996

Regulation of beta-glucosidase biosynthesis in Aspergillus nidulans.

beta-Glucosidase in Aspergillus nidulans was found to be both intracellular and extracellular. The intracellular beta-glucosidase was synthesized after the exhaustion of carbon source in the medium. The extracellular enzyme appeared with autolysis of the mycelium. Biosynthesis of beta-glucosidase was not induced by various carbohydrates but repressed to varying extents in the presence of glucose, glycerol, and 2-deoxyglucose. This repression was not relieved by addition of cAMP. The repression was relieved much more by mutations in the creA gene than by one in the creC gene. Thus, beta-glucosidase synthesis in A. nidulans is subject to carbon catabolite repression.

Aspergillus nidulans↗
PubMed2005

Levels and activity of the Pseudomonas putida global regulatory protein Crc vary according to growth conditions.

The global regulatory protein Crc is involved in the repression of several catabolic pathways for sugars, hydrocarbons, and nitrogenated and aromatic compounds in Pseudomonas putida and Pseudomonas aeruginosa when other preferred carbon sources are present in the culture medium (catabolite repression), therefore modulating carbon metabolism. We have analyzed whether the levels or the activity of Crc is regulated. Crc activity was followed by its ability to inhibit the induction by alkanes of the P. putida OCT plasmid alkane degradation pathway when cells grow in a complete medium, where the effect of Crc is very strong. The abundance of crc transcripts and the amounts of Crc protein were higher under repressing conditions than under nonrepressing conditions. The presence of crc on a high-copy-number plasmid considerably increased Crc levels, but this impaired its ability to inhibit the alkane degradation pathway. Crc shows similarity to a family of nucleases that have highly conserved residues at their catalytic sites. Mutation of the corresponding residues in Crc (Asp220 and His246) led to proteins that can inhibit induction of the alkane degradation pathway when present at normal or elevated levels in the cell. Repression by these mutant proteins occurred only under repressing conditions. These results suggest that both the amounts and the activity of Crc are modulated and support previous proposals that Crc may form part of a signal transduction pathway. Furthermore, the activity of the mutant proteins suggests that Crc is not a nuclease.

Bacterial Proteins↗
PubMed1993

Construction of glucose-repressible yeast expression vectors.

A set of two episomal yeast expression vectors, pYME1 and pYME2, were constructed. These Saccharomyces cerevisiae-Escherichia coli shuttle vectors each contain a modified yeast MAL6S (encoding maltase) promoter that is expressed constitutively, but is subject to carbon catabolite repression by glucose. Expression from this promoter is still dependent upon the presence of active MALR (regulatory) protein. These expression vectors are particularly useful because most S. cerevisiae strains are MAL+, thereby exhibiting a wider host range than GAL-based vector systems. These pYME1 and pYME2 vectors are capable of expression to levels comparable to GAL-based expression plasmids and much higher than a variety of other repressible promoter vectors. The vectors are identical, except that their multiple cloning sites (MCS) are in opposite orientations, making them convenient for inserting heterologous genes.

Base Sequence↗
PubMed1999

Glycerol-3-phosphate-mediated repression of malT in Escherichia coli does not require metabolism, depends on enzyme IIAGlc and is mediated by cAMP levels.

malT encodes the central activator of the maltose system in Escherichia coli, a gene that is typically under positive control of the cAMP/CAP catabolite repression system. When cells were grown in tryptone broth, the addition of glycerol reduced malT expression two- to threefold. Phosphorylation of glycerol to glycerol-3-phosphate (G3P) was necessary for this repression, but further metabolism to dihydroxyacetone phosphate was not. Mutants lacking adenylate cyclase and harbouring a crp* mutation (synthesizing a cAMP receptor protein that is independent of cAMP) no longer repressed a transcriptional malT-lacZ fusion but still repressed a translational malT-lacZ fusion. Similar results were obtained with a mutant lacking enzyme IIAGlc. For the translational fusion (in a cya crp* genetic background) to be repressed by glycerol, a drop to pH 5 of the growth medium was necessary. Thus, while transcriptional repression by glycerol requires enzyme IIAGlc, cAMP and CAP, pH-mediated translational repression is cAMP independent. Other sugars that are not transported by the phosphotransferase system, most notably D-xylose, showed the same effect as glycerol.

Artificial Gene Fusion↗
PubMed2006

Effect of HPr phosphorylation on structure, dynamics, and interactions in the course of transcriptional control.

The serine46-phosphorylated form of the bacterial protein HPr fulfils an essential function in carbon catabolite repression (CCR). Using molecular dynamics (MD) we studied the effect of Ser46 phosphorylation on the molecular properties of HPr and its capability to act as the co-repressor of carbon catabolite protein A (CcpA). The calculated pK (a) values for a representative set of HPr(Ser46P) structures indicate that the phosphate group of HPr(Ser46P) exists predominantly in the unprotonated form under neutral conditions. A hydrogen bond detected in HPr(Ser46P) between one phosphate-group oxygen and a side-chain hydrogen of Asn43-an amino acid conserved in all HPr proteins of Gram-positive bacteria that regulate their carbon consumption by CCR-might fulfil an important role in CcpA-HPr(Ser46P) complex formation. MD simulations show that the Ser46P-Asn43 hydrogen bond present in the unbound structure is replaced by intermolecular interactions upon complex formation. The degree to which amino acids in the CcpA-HPr(Ser46P) interface contribute to cofactor binding was analyzed by in silico alanine scanning. Lys307, Arg303, Asp296, Val300, and Tyr295 of CcpA were identified as important amino acids for the CcpA-HPr(Ser46P) interaction. Three of these residues are directly involved in sensing the correct phosphorylation state at His15(HPr) and Ser46(HPr). A substitution of interface residues Val319, Val314, Ser316, Leu321 and Gln320 by alanine showed that these amino acids, which contact helix alpha2 of HPr(Ser46P), play a less prominent role for complex formation.

Amino Acid Substitution↗
PubMed2002

The transcriptional regulation of the Streptococcus mutans bgl regulon.

A beta-glucoside utilization regulon recently isolated from Streptococcus mutans has been shown to contain genes involved in beta-glucoside hydrolysis and a putative regulator. The bglP gene encodes a beta-glucoside-specific enzyme II (EII) component of the phosphoenolpyruvate-dependent phosphotransferase system, the bglC gene encodes a putative transcriptional regulator, and the bglA gene encodes a putative phospho-beta-glucosidase. To investigate the transcriptional activity of these genes, the putative promoter regions of the bglP, bglC and bglA genes were fused with the E. coli lacZ reporter gene. The resultant reporter plasmids were used to monitor the transcriptional activity of these loci in S. mutans. The results illustrate that these genes are not repressed by glucose in the presence of an inducing beta-glucoside, esculin, to the levels of expression observed in the absence of esculin. Therefore, these loci are not subject to catabolite repression by glucose to noninduced levels of expression. The bglC gene product was determined to be a positive transcriptional regulator of the bglA gene but does not regulate the expression of the bglP gene. Thus, regulation of these loci requires different and multiple control mechanisms.

Cloning, Molecular↗
PubMed1965

REPRESSION OF TRYPTOPHANASE SYNTHESIS IN ESCHERICHIA COLI.

Beggs, William H. (University of Cincinnati, Cincinnati, Ohio), and Herman C. Lichstein. Repression of tryptophanase synthesis in Escherichia coli. J. Bacteriol. 89:996-1004. 1965.-The nature of the glucose effect on tryptophanase in Escherichia coli (Crookes) was investigated to test the catabolite-repression hypothesis. Under static conditions of growth in the presence of 0.005 m glucose, tryptophanase was repressed and remained so upon continued static incubation subsequent to glucose exhaustion. Aeration following glucose exhaustion under static cultural conditions resulted in rapid enzyme synthesis. In the absence of glucose, certain amino acids repressed tryptophanase synthesis early in the growth cycle under aerated conditions. An inverse relationship was observed between the concentration of acid-hydrolyzed casein and the level of tryptophanase. At 3 hr, enzyme activity in cells grown in media containing 0.05% acid-hydrolyzed casein was at least five times that of cells grown in the presence of 1% casein. Addition of 0.005 m d- or l-serine to a 0.05% acid-hydrolyzed casein medium rendered the medium capable of strongly repressing tryptophanase. Glucose-expended medium was prepared by allowing cells to grow and exhaust glucose in static culture. When this expended medium was recovered and inoculated with fresh cells not previously exposed to glucose, tryptophanase synthesis was repressed for a short period in shake culture, but in static culture enzyme synthesis was only slightly affected. When the expended medium was prepared from shake cultures, fresh cells were not repressed strongly when subsequent incubation was carried out aerobically. The tryptophan pool in glucose-repressed cells grown in shake culture was appreciably less than in cells grown in the absence of glucose or in cells undergoing synthesis of tryptophanase after exhaustion of the sugar.

Amino Acids↗
PubMed1992

The UGA43 negative regulatory gene of Saccharomyces cerevisiae contains both a GATA-1 type zinc finger and a putative leucine zipper.

The UGA43 gene of Saccharomyces cerevisiae is required for repression of inducible genes involved in the utilization of 4-aminobutyric acid (GABA) or urea as nitrogen sources. The UGA43 gene has been cloned by complementation of a uga43 mutation. The N-terminal region of the UGA43 protein is very similar to the DNA-binding zinc-finger region typical of the GATA regulatory factor family in vertebrates. UGA43 is the first reported instance of a GATA protein with a negative regulatory function. The C-terminal region of the predicted UGA43 protein contains a putative leucine zipper. Sequencing of three uga43 mutant alleles suggests that the GATA and putative leucine-zipper regions are both required for the repressive activity of UGA43. UGA43 appears to be a highly regulated gene. On "poor" nitrogen sources, UGA43 transcripts are measured at high levels whereas they are nearly undetectable in conditions of nitrogen catabolite repression. The levels measured on "poor" nitrogen sources are further increased in uga43 mutant cells, suggesting that UGA43 exerts negative autoregulation.

Amino Acid Sequence↗
PubMed2003

PaeX, a second pectin acetylesterase of Erwinia chrysanthemi 3937.

Erwinia chrysanthemi causes soft-rot diseases of various plants by enzymatic degradation of the pectin in plant cell walls. Pectin is a complex polysaccharide. The main chain is constituted of galacturonate residues, and some of them are modified by methyl and/or acetyl esterification. Esterases are necessary to remove these modifications and, thus, to facilitate the further degradation of the polysaccharidic chain. In addition to PaeY, the first pectin acetylesterase identified in the E. chrysanthemi strain 3937, we showed that this bacterium produces a second pectin acetylesterase encoded by the gene paeX. The paeX open reading frame encodes a 322-residue precursor protein of 34,940 Da, including a 21-amino-acid signal peptide. Analysis of paeX transcription, by using gene fusions, revealed that it is induced by pectic catabolic products and affected by catabolite repression. The expression of paeX is regulated by the repressor KdgR, which controls all the steps of pectin catabolism; by the repressor PecS, which controls most of the pectinase genes; and by catabolite regulatory protein, the global activator of sugar catabolism. The paeX gene is situated in a cluster of genes involved in the catabolism and transport of pectic oligomers. In induced conditions, the two contiguous genes kdgM, encoding an oligogalacturonate-specific porin, and paeX are both transcribed as an operon from a promoter proximal to kdgM, but transcription of paeX can also be uncoupled from that of kdgM in noninduced conditions. PaeX is homologous to the C-terminal domain of the Butyrivibrio fibriosolvens xylanase XynB and to a few bacterial esterases. PaeX contains the typical box (GxSxG) corresponding to the active site of the large family of serine hydrolases. Purified PaeX releases acetate from various synthetic substrates and from sugar beet pectin. The PaeX activity increased after previous depolymerization and demethylation of pectin, indicating that its preferred substrates are nonmethylated oligogalacturonides. PaeX is mostly found in the periplasmic space of E. chrysanthemi. These data suggest that PaeX is mainly involved in the deacetylation of esterified oligogalacturonides that enter the periplasm by the KdgM porin.

Amino Acid Sequence↗
PubMed1992

Integration host factor facilitates repression of the put operon in Salmonella typhimurium.

Transcriptional regulation of the put operon is mediated by a unique mechanism involving autogenous regulation by the PutA protein, a membrane-associated dehydrogenase. The 420-bp put control region contains the putP and putA promoters, multiple operator sites, multiple catabolite repression protein binding sites, and several potential integration host factor (IHF)-binding sites (ihf). In this study, we show that IHF facilitates repression of the put operon in vivo, and IHF binds specifically to two ihf sites in the put control region in vitro. DNA gyrase mutants that alter the degree of chromosomal supercoiling do not affect put regulation, indicating that the effect of IHF on put expression is in this case independent of supercoiling.

Amino Acid Sequence↗