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At least 703 records · Page 39Linked to original sources
PubMed1994

A reporter gene analysis of penicillin biosynthesis gene expression in Penicillium chrysogenum and its regulation by nitrogen and glucose catabolite repression.

Vectors which possess a truncated niaD gene encoding nitrate reductase were developed to allow targeted gene integration during transformation of an niaD mutant Penicillium chrysogenum host. The Penicillium genes pcbC and penAB are immediately adjacent to each other and are divergently transcribed, with an intergenic control region serving as their promoters. Gene fusions were constructed with a reporter gene, uidA, which encodes beta-glucuronidase. The pcbC-penAB intergenic region was fused to the uidA gene in both orientations so that regulated expression of each structural gene could be investigated. These fusion genes were targeted to the chromosomal site of the niaD locus of P. chrysogenum, and their expression was examined under different growth conditions. The expression of each of these penicillin biosynthesis genes was found to be regulated by nitrogen repression, glucose repression, and growth stage control.

Base Sequence↗
PubMed1980

Regulation of aromatic amino acid biosynthesis in Escherichia coli K-12: control of the aroF-tyrA operon in the absence of repression control.

Evidence was found which indicated that a mutation in gene trpS affected the rate of synthesis of tyrosine-repressible 3-deoxy-D-arabinoheptulosonic acid-7-phosphate (DAHP) synthetase. The effect was found to occur independently of repression mediated by the tyrR gene product, and it was not due to a change in growth rate, nor was it a manifestation of the stringent response. It is proposed that in the proximal region of the aroF-tyrA operon there is an attenuator site controlled by the level of charged tryptophanyl-transfer RNA. In addition, it was demonstrated that starvation for certain amino acids led to degradation of tyrosine-repressible DAHP synthetase, but not phenylalanine-repressible DAHP synthetase, and supplementation with the missing amino acid led to an increased rate of synthesis of tyrosine-repressible DAHP synthetase during subsequent growth.

Amino Acids↗
PubMed1997

Contribution of glucose kinase to glucose repression of xylose utilization in Bacillus megaterium.

The glk gene from Bacillus megaterium, which encodes glucose kinase, was isolated and analyzed. Disruption by a transcriptional glk-luxAB fusion indicated that glk is the only glucose kinase gene in that strain but did not affect growth of that mutant on glucose. Determination of luciferase activity under various growth conditions revealed constitutive transcription of glk. Expression of a xylA-lacZ fusion was repressed by glucose in the strain with the glk disruption about twofold less efficiently than in the wild type. The potential contribution of glk expression to glucose repression is discussed.

Amino Acid Sequence↗
PubMed1996

Disruption of the NAD(+)-specific glutamate dehydrogenase gene of Neurospora crassa by means of the RIP (repeat-induced point mutations) process.

The structural gene for the catabolite-repressed, substrate-induced NAD(+)-specific glutamate dehydrogenase (gdh-1) of Neurospora crassa was disrupted using the process of repeat-induced point mutation (RIP). Plasmids containing incomplete copies of the gene, along with selectable markers, were introduced into germinated conidia by electroporation. The sexual progeny of a transformant containing an ectopically integrated copy of a plasmid, harbouring the 5' flanking region and a part of the coding sequence of gdh-1 DNA, was examined for the occurrence of RIP by (i) Southern blot analysis of the genomic DNA digested with the isoschizomers MboI and Sau3A, (ii) Northern blot analysis of total RNA in cultures subjected to repression and induction conditions for NAD-GDH, (iii) direct assessment of enzymatic activity, and (iv) evaluation of protein levels by Western blot analysis using a polyclonal anti-GDH IgG preparation. Attempts were made at delineating different regions of the gene exhibiting RIP by using 32P-labelled DNA probes, corresponding to (i) the complete gene, (ii) a fragment containing the 5' flanking region plus two-thirds of the coding sequence, and (iii) the 5' flanking segment alone. The extent and relative location of RIP, as revealed by these hybridization probes, appeared to correlate with changes in specific activity under repression and derepression conditions. Mutant progeny, thus recovered, included isolates with altered regulatory features, such as constitutive expression, inability to elicit derepression, higher-than-wildtype GDH levels under derepression and inefficient repression.

Blotting, Northern↗
PubMed1987

Arginine-specific carbamoyl phosphate metabolism in mitochondria of Neurospora crassa. Channeling and control by arginine.

Citrulline is synthesized in mitochondria of Neurospora crassa from ornithine and carbamoyl phosphate. In mycelia grown in minimal medium, carbamoyl phosphate limits citrulline (and arginine) synthesis. Addition of arginine to such cultures reduces the availability of intramitochondrial ornithine, and ornithine then limits citrulline synthesis. We have found that for some time after addition of excess arginine, carbamoyl phosphate synthesis continued. Very little of this carbamoyl phosphate escaped the mitochondrion to be used in the pyrimidine pathway in the nucleus. Instead, mitochondrial carbamoyl phosphate accumulated over 40-fold and turned over rapidly. This was true in ornithine- or ornithine carbamoyltransferase-deficient mutants and in normal mycelia during feedback inhibition of ornithine synthesis. The data suggest that the rate of carbamoyl phosphate synthesis is dependent to a large extent upon the specific activity of the slowly and incompletely repressible synthetic enzyme, carbamoyl-phosphate synthetase A. In keeping with this conclusion, we found that when carbamoyl-phosphate synthetase A was repressed 2-10-fold by growth of mycelia in arginine, carbamoyl phosphate was still synthesized in excess of that used for residual citrulline synthesis. Again, only a small fraction of the excess carbamoyl phosphate could be accounted for by diversion to the pyrimidine pathway. The continued synthesis and turnover of carbamoyl phosphate in mitochondria of arginine-grown cells may allow rapid resumption of citrulline formation after external arginine disappears and no longer exerts negative control on ornithine biosynthesis.

Arginine↗
PubMed1970

Repression of phenolic acid-synthesizing enzymes and its relation to iron uptake in Bacillus subtilis.

Excretion of the metal-chelating phenolic acid, 2,3-dihydroxybenzoate, by a tryptophan-requiring strain (M-13) of Bacillus subtilis was inversely proportional to the iron added to the medium. Addition of iron as the ferric chelates of two secondary hydroxamates (ferri-schizokinen and Desferal) markedly reduced excretion. Synthesis of 2,3-dihydroxybenzoate from chorismate by extracts of B. subtilis M-13, grown in low-iron medium, was unaltered by additions of FeSO(4), FeCl(3), ferrischizokinen, 2,3-dihydroxybenzoate, the 2,3-dihydroxybenzoate-iron complex, or by extracts of cells grown in high-iron medium (which contained no demonstrable 2,3-dihydroxybenzoate-synthesizing activity) to the extracts of "low-iron cells." Iron control seemed to involve repression of synthesis of the enzymes in the 2,3-dihydroxybenzoate pathway. Both ferri-schizokinen and 2,3-dihydroxybenzoate plus iron enhanced considerably the otherwise minimal repressive effects of iron at low concentrations. Ferri-schizokinen delayed derepression of the pathway in B. subtilis M-13, and reduced its rate of synthesis after derepression. Addition of FeSO(4) to derepressed cells of B. subtilis M-13 halted synthesis of the enzymes after a lag period. The effect of the ferric hydroxamates was related to the capacity of B. subtilis M-13 to incorporate (59)Fe(3+) from Desferal-(59)Fe(3+). Cellular accumulation of (59)Fe(3+) from Desferal-(59)Fe(3+) after 20 min was nearly double that incorporated from (59)FeCl(3).

Bacillus subtilis↗