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Query: KEGG:D03345 (beta-Galactosidase)
 434 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

beta-Galactosidase and tryptophanase were induced either simultaneously or successively during continuous cultivation of the inducible strain Escherichia coli K 12 in the chemostat. Growth was limited by glycerol and the dilution rate was 0.1 h-1. During both the simultaneous and successive induction specific rates of synthesis, as well as maximum enzyme levels, were identical with those obtained after independent induction of individual enzymes. As compared with batch cultivation, beta-galactosidase reached the same specific rate of synthesis in the chemostat, whereas the specific rate of synthesis of tryptophanase in the chemostat was up to five times higher.
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PMID:Simultaneous and successive induction of synthesis of beta-galactosidase and tryptophanase in Escherichia coli K 12 in the chemostat. 33 Mar 63

Recombinant DNA and genetic techniques were used to construct Escherichia coli strains SOH92 [phi(cls-lacZ+)] and SOH93 [phi(cls-'lacZ)hyb]. beta-Galactosidase (116 kDa) synthesized by strain SOH92 was primarily present in the particulate fraction. Strain SOH92 produced about 20-fold more beta-galactosidase activity than strain SOH93. Expression of clsphilacZ in both SOH92 and SOH93 was influenced by the terminal electron acceptor (increasing in the order oxygen, nitrate, fumarate) when the cells were cultured in minimal medium with glycerol as the sole carbon source. As strains SOH92 and SOH93 progressed from early to late log growth phase under aerobic conditions in LB broth, clsphilacZ expression increased about 2.5-fold. Fusion strains containing a pss-1 allele had an increased cardiolipin (CL) level, but no corresponding increase in clsphilacZ expression was observed. A cls::Tn10dTet null mutation was introduced into SOH92 and SOH93. The strains produced less CL, but no corresponding changes in clsphilacZ expression were observed. A high copy number plasmid bearing the cls gene had no effect on clsphilacZ expression. Taken together, these results indicate that cls is not subject to autogenous regulation.
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PMID:Genetic regulation of cardiolipin synthase in Escherichia coli. 166 9

Expression of the glpA operon encoding the extrinsic membrane anaerobic sn-glycerol-3-phosphate dehydrogenase complex of Escherichia coli K-12 was studied in five strains carrying independent glpA-lac operon fusions. The location of the fusions was confirmed by transduction. Two of the strains produced an enzymatically active anaerobic sn-glycerol-3-phosphate dehydrogenase that accumulated in the cytoplasmic fraction of the cells. This suggests the loss of a specific membrane anchor subunit encoded by a distal gene, glpB, which was disrupted by the insertion. beta-Galactosidase in all five strains carrying phi(glpA-lac) was highly inducible by glycerol only anaerobically. A mutation in fnr, a pleiotropic activator gene, prevented full induction of the phi(glpA-lac), demonstrating that the Fnr protein is a positive regulator of the primary dehydrogenase as well as of the terminal reductases of anaerobic respiratory chains. Low concentrations of the respiratory poison KCN had a permissive effect on aerobic expression of phi(glpA-lac). Aerobic expression of the hybrid operon was also enhanced in isogenic derivatives of the fusion strains deficient in protoporphyrin biosynthesis (hemA). Thus, heme proteins may play a role in mediating aerobic repression of the anaerobic respiratory chain.
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PMID:Use of phi(glp-lac) in studies of respiratory regulation of the Escherichia coli anaerobic sn-glycerol-3-phosphate dehydrogenase genes (glpAB). 636 89

Expression of the Aspergillus nidulans brlA gene plays a fundamental role in the switch from vegetative growth to asexual reproduction. Using a media-shifting protocol to induce submerged sporulation and brlA-lacZ as an expression marker, it was shown that carbon and nitrogen starvation stress induced brlA transcription to different degrees. Glucose starvation induced briA rapidly to high levels and resulted in spore formation on reduced conidiophores, whereas nitrogen starvation induced brlA gradually to lower levels and sporulation occurred to a lesser extent but from more complex conidiophores. beta-Galactosidase activity paralleled brlA alpha and brlA beta mRNA. No clear qualitative differences between the two brlA transcripts were found in these starvation conditions, suggesting that the different patterns of sporulation could be explained by quantitative expression differences. Since brlA mRNA did not accumulate in the presence of a high glucose concentration, we investigated the role of other carbon sources on brlA expression. Non-repressing carbon sources such as glycerol, acetate and arabinose were as effective as glucose in preventing brlA mRNA accumulation, suggesting that the glucose effects on brlA expression could be explained as a response to nutrient starvation, rather than by carbon catabolite repression. Despite similar low levels of brlA transcripts being detected during growth in glucose or non-repressing carbon sources, conidiophores were formed only in medium containing glycerol, acetate or arabinose. When mycelia were not shifted to starvation conditions, sporulation was not observed in standard minimal medium even after glucose was exhausted, unless the medium was buffered.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Starvation stress modulates the expression of the Aspergillus nidulans brlA regulatory gene. 789 14

Expression of the Bacillus subtilis glpD gene which encodes glycerol-3-phosphate (G3P) dehydrogenase is regulated by the GlpP protein which, in the presence of G3P, causes antitermination of transcription of glpD. The glpD gene leader fused to lacZ was integrated into the chromosome of Escherichia coli deleted for the lac operon and carrying the B. subtilis glpP gene on a plasmid. beta-Galactosidase activity of this strain was increased by the addition of G3P. When G3P and glucose, glucose-6-phosphate or fructose-6-phosphate were added, beta-galactosidase activity was reduced showing that GlpP mediates catabolite repression of transcription from the glpD leader in the absence of any other B. subtilis protein.
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PMID:The Bacillus subtilis glpD leader and antiterminator protein GlpP provide a target for glucose repression in Escherichia coli. 959 68

Growth and beta-galactosidase activity of the penicillin producer industrial Penicillium chrysogenum NCAIM 00237 strain were examined using different carbon sources. Good growth was observed using glucose, sucrose, glycerol and galactose, while growth on lactose was substantially slower. beta-Galactosidase activity was high on lactose and very low on all the other carbon sources tested. In glucose grown cultures after exhaustion of glucose as repressing carbon source a derepressed low level of the enzyme was observed. cAMP concentration in lactose grown cultures was relatively high, in glucose grown cultures was low. Caffeine substantially decreased glucose consumption and growth but did not increase beta-galactosidase activity and did not prevent glucose repression which rules out the involvement of cAMP in the regulation of beta-galactosidase biosynthesis in Penicillium chrysogenum.
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PMID:Carbon source regulation of beta-galactosidase biosynthesis in Penicillium chrysogenum. 1180 45

The regulation of formation of the single intracellular beta-galactosidase activity of Aspergillus nidulans was investigated. beta-Galactosidase was not formed during growth on glucose or glycerol, but was rapidly induced during growth on lactose or D-galactose. L-Arabinose, and -- with lower efficacy -- D-xylose also induced beta-galactosidase activity. Addition of glucose to cultures growing on lactose led to a rapid decrease in beta-galactosidase activity. In contrast, in cultures growing on D-galactose, addition of glucose decreased the activity of beta-galactosidase only slightly. Glucose inhibited the uptake of lactose, but not of D-galactose, and required the carbon catabolite repressor CreA for this. In addition, CreA also repressed the formation of basal levels of beta-galactosidase and partially interfered with the induction of beta-galactosidase by D-galactose, L-arabinose, and D-xylose. D-Galactose phosphorylation was not necessary for beta-galactosidase induction, since induction by D-galactose occurred in an A. nidulans mutant defective in galactose kinase, and by the non-metabolizable D-galactose analogue fucose in the wild-type strain. Interestingly, a mutant in galactose-1-phosphate uridylyl transferase produced beta-galactosidase at a low, constitutive level even on glucose and glycerol and was no longer inducible by D-galactose, whereas it was still inducible by L-arabinose. We conclude that biosynthesis of the intracellular beta-galactosidase of A. nidulans is regulated by CreA, partially repressed by galactose-1-phosphate uridylyl transferase, and induced by D-galactose and L-arabinose in independent ways.
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PMID:Regulation of formation of the intracellular beta-galactosidase activity of Aspergillus nidulans. 1247 99

The significance of the chronicled role of the yeast transcription factor Adr1p in regulating ETR1 was examined in wild type and isogenic adr1Delta mutant cells. An ETR1-lacZ reporter construct was used to verify Adr1p-dependent gene expression. On solid glycerol medium containing X-gal, wild-type cells expressing the reporter turned blue, whereas the adr1Delta mutants remained white. beta-Galactosidase activity measurements following 24-h cell growth in liquid glycerol medium revealed a 6.5-fold greater expression level of the reporter gene in the wild type compared with the adr1Delta mutant. In contrast, immunoblotting showed that Etr1p abundance was essentially indistinguishable between the two strains whereas Cta1p, whose expression depends on Adr1p, was present in the wild-type cells, but not in the mutants. Moreover, enzyme assays conducted on transformed wild-type and adr1Delta mutant cells expressing a plasmid-borne ETR1 tethered behind the native promoter revealed similar levels of reductase activity, and the lipoic acid content in the two parental strains was equivalent. Hence, while Adr1p influenced the transcription levels of ETR1, it did not alter the abundance of Etr1p, the level of reductase activity, or the cellular amount of lipoic acid. The results point toward a potentially novel layer of control for maintaining physiological levels of lipoic acid.
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PMID:A novel circuit overrides Adr1p control during expression of Saccharomyces cerevisiae 2-trans-enoyl-ACP reductase Etr1p of mitochondrial type 2 fatty acid synthase. 1958 90