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1.
Jacqueline Deschamps Evelyne Dubois Jean-Marie Wiame 《Molecular & general genetics : MGG》1979,174(3):225-232
Summary The ornithine transaminase (EC.2.6.1.13) of Saccharomyces cerevisiae is induced by arginine, ornithine, and their analogs. Genetic regulatory elements which are involved in this induction process have been defined due to the isolation of specific mutants. Two classes of OTAse operator mutants have previously been described; three unlinked genes are presumed to code for a specific repressor, CARGR of both of the arginine catabolic enzymes, arginase, and ornithine transaminase. The level of transaminase of cells grown on ammonia plus arginine is much lower than it is when arginine is the sole nitrogen source. Ammonia thus seems to limit the amount of enzyme synthesized when arginine is present in the growth medium. Nevertheless, all attempts to disclose a nitrogen catabolite repression process in OTAse synthesis have failed; neither the action of mutations that release this regulation on arginase and other catabolic enzymes, nor the use of derepressing growth conditions, affect OTAse synthesis. A decrease of the cells' arginine pool when amonia or aminoacids (serine, glutamate) are added to arginine as a nitrogen nutrient results in a progressive reduction of transaminase synthesis. This suggests that arginine is the only physiological effector in those conditions: ammonia or some aminoacids would reduce the enzyme synthesis because of an inducer exclusion. The first stage of OTAse induction would then be operated by the CARGR repressor, and an additional regulatory element might take part in the full scale process. Preliminary data favoring the involvment of such an element are presented. 相似文献
2.
Under various conditions of growth of the methylotrophic yeast Hansenula polymorpha, a tight correlation was observed between the levels of flavin adenine dinucleotide (FAD)-containing alcohol oxidase, and the levels of intracellularly bound FAD and flavin biosynthetic enzymes. Adaptation of the organism to changes in the physiological requirement for FAD was by adjustment of the levels of the enzymes catalyzing the last three steps in flavin biosynthesis, riboflavin synthetase, riboflavin kinase and flavin mononucleotide adenylyltransferase. The regulation of the synthesis of the latter enzymes in relation to that of alcohol oxidase synthesis was studied in experiments involving addition of glucose to cells of H. polymorpha growing on methanol in batch cultures or in carbon-limited continuous cultures. This resulted not only in selective inactivation of alcohol oxidase and release of FAD, as previously reported, but invariably also in repression/inactivation of the flavin biosynthetic enzymes. In further experiments involving addition of FAD to the same type of cultures it became clear that inactivation of the latter enzymes was not caused directly by glucose, but rather by free FAD that accumulated intracellularly. In these experiments no repression or inactivation of alcohol oxidase occurred and it is therefore concluded that the synthesis of this enzyme and the flavin biosynthetic enzymes is under separate control, the former by glucose (and possibly methanol) and the latter by intracellular levels of free FAD.Abbreviations FAD
Flavin adenine dinucleotide
- FMN
riboflavin-5-phosphate; flavin mononucleotide
- Rf
riboflavin 相似文献
3.
J. L. Smith M. M. Bencivengo R. L. Buchanan C. A. Kunsch 《Archives of microbiology》1986,144(2):131-136
In this study, we investigated the relationship between carbohydrate metabolism and repression of staphylococcus enterotoxin A (SEA) in Staphylococcus aureus 196E and a pleiotrophic mutant derived from strain 196E. The mutant, designated at strain 196E-MA, lacked a functional phosphoenolpyruvate phosphotransferase system (PTS). The mutant produced acid, under aerobic conditions, from only glucose and glycerol. The parent strain contained an active PTS, and aerobically produced acid from a large number of carbohydrates. Prior growth in glucose led to repression of SEA synthesis in the parent strain; addition to the casamino acids enterotoxin production medium (CAS) led to more severe repression of toxin synthesis. The repression was not related to pH decreases produced by glucose metabolism. When S. aureus 196E was grown in the absence of glucose, there was inhibition of toxin production as glucose level was increased in CAS. The inhibition was related to pH decrease and was unlike the repression observed with glucose-grown strain 196E. The inhibition of SEA synthesis in mutant strain 196E-MA was approximately the same in cells grown with or without glucose and was pH related. Repression of SEA synthesis similar to that seen with glucose-grown S. aureus 196E could not be demonstrated in the mutant. In addition, glucose-grown S. aureus 196E neither synthesized -galactosidase nor showed respiratory activity with certain tricarboxylic acid (TCA) cycle compounds. Glucose-grown strain 196E-MA, however, did not show supressed respiration of TCA cycle compounds; -galactosidase was not synthesized because the mutant lacked a functional PTS. Cyclic adenosine-3, 5-monophosphate did not reverse the repression by glucose of SEA or -galactosidase synthesis in glucose-grown S. aureus 196E. An active PTS appears to be necessary to demonstrate glucose (catabolite) repression in S. aureus.Abbreviations SEA
staphylococcal enterotoxin A
- SEB
staphylococcal enterotoxin B
- SEC
staphylococcal enterotoxin C
- PTS
phosphoenolpyruvate phosphotransferase system
- CAS
casamino acids salts medium
- TCA
tricarboxylic acid cycle 相似文献
4.
Summary Catabolic effects which exert control over the inducible synthesis of three enzymes in Arthrobacter crystallopoietes involve at least three different mechanisms: interference with inducer transport, severe catabolite repression, and transient repression. The rate of histidase induction by histidine is reduced by incubation of the cells with succinate or glucose. The maximum effect of succinate, 67% reduction in histidase production, occurs only after 100 min of incubation with succinate. At least 3h of incubation are required for the maximum effect of glucose (31% reduction in enzyme induction). Both succinate and glucose inhibit histidine transport. Cyclic adenosine 3,5-monophosphate (cyclic AMP), at 10-7 M, slightly stimulates the induction of histidase in cultures both with or without succinate. No conditions were found in which cyclic AMP abolishes the effect of succinate. Induction of l-serine dehydratase by glycine is severely and permanently repressed by glucose and to a lesser extent by citrate. Glucose does not affect glycine uptake. Succinate, fumarate, and aspartate, which are all better substrates than glucose or citrate for growth of A. crystallopoietes, have no effect on l-serine dehydratase induction. Induction and repression of l-serine dehydratase are not affected by cyclic AMP. Synthesis of isocitrate lyase after addition of acetate is unaffected by glucose but is severely repressed by succinate or fumarate. Aspartate and glutamate cause a transient repression of enzyme synthesis after which synthesis proceeds at the control rate. The ability to transport acetate is inducible. Development of this capacity in the presence of acetate is not affected by succinate or glutamate. Cyclic AMP has no effect on enzyme production or repression. A. crystallopoietes takes up radioactive cyclic AMP and has at least one of the enzymes of cyclic AMP metabolism, adenyl cyclase. 相似文献
5.
Summary Two kinds of mutants of Aspergillus nidulans with altered response of arginine catabolic enzymes to glucose and ammonium repression were obtained. Mutations in the suF locus result in the insensitivity of these enzymes to glucose and to one type of ammonium repression. Mutations in the AniA locus result in hypersensitivity to both types of repression. The enzymes studied can be induced by arginine in AniA mutants only when glucose or the nitrogen source is removed from the medium. The suF mutations are recessive while AniA are dominant. Double suF AniA mutants retain only the suF properties. The functions of both genes and their interrelations are discussed. 相似文献
6.
In Phanerochaete chrysosporium fruit body formations is subject to strong catabolite repression by glucose in the presence of physiological levels of nitrogen. Walseth cellulose was found to be the best source of carbon for the induction of fruit body and consequent basidiospore synthesis. Ejected basidiospores collected from cultures grown under these conditions for two weeks are contaminated with neither conidia nor mycelial fragments and are therefore suitable for genetic analysis of recombination. Under conditions of nitrogen limitation, the glucose catabolite repression of fruit body synthesis was relieved. Exogenous adenosine 3,5-monophosphate but not other related nucleotides, also relieved glucose catabolite repression of fruit body formation. 相似文献
7.
Two glucose-phosphorylating enzymes, a hexokinase phosphorylating both glucose and fructose, and a glucose-specific glucokinase
were electrophoretically separated in the methylotrophic yeastHansenula polymorpha. Hexokinase-negative mutants were isolated inH. polymorpha by using mutagenesis, selection and genetic crosses. Regulation of synthesis of the sugar-repressed alcohol oxidase, catalase
and maltase was studied in different hexose kinase mutants. In the wild type and in mutants possessing either hexokinase or
glucokinase, glucose repressed the synthesis of maltase, alcohol oxidase and catalase. Glucose repression of alcohol oxidase
and catalase was abolished in mutants lacking both glucose-phosphorylating enzymes (i.e. in double kinase-negative mutants). Thus, glucose repression inH. polymorpha cells requires a glucose-phosphorylating enzyme, either hexokinase or glucokinase. The presence of fructose-phosphorylating
hexokinase in the cell was specifically needed for fructose repression of alcohol oxidase, catalase and maltase. Hence, glucose
or fructose has to be phosphorylated in order to cause repression of the synthesis of these enzymes inH. polymorpha suggesting that sugar repression in this yeast therefore relies on the catalytic activity of hexose kinases. 相似文献
8.
Tobias Habicher Arian John Niklas Scholl Andreas Daub Tobias Klein Priya Philip Jochen Büchs 《Biotechnology and bioengineering》2019,116(6):1326-1340
To overcome catabolite repression, industrial fermentation processes are usually operated in substrate-limited fed-batch mode. Therefore, the implementation of such an operating mode at small scale is crucial to maintain comparable process conditions. In this study, Bacillus licheniformis, a well-known producer of proteases, was cultivated with carbon (glucose)- and nitrogen (ammonium)-limited fed-batch conditions using the previously introduced membrane-based fed-batch shake flasks. A repression of protease production by glucose and ammonium was thus avoided and yields increased 1.5- and 2.1-fold relative to batch, respectively. An elevated feeding rate of glucose caused depletion of ammonium, which was recognizable within the oxygen transfer rate (OTR) signal measured with the Respiration Activity MOnitoring System (RAMOS). Ammonium limitation was prevented by feeding ammonium simultaneously with glucose. The OTR signal clearly indicated the initiation of the fed-batch phase and gave direct feedback on the nutrient release kinetics. Increased feeding rates of glucose and ammonium led to an elevated protease activity without affecting the protease yield (YP/Glu). In addition to YP/Glu, protease yields were determined based on the metabolized amount of oxygen . The results showed that the protease production correlated with the amount of consumed glucose as well as with the amount of consumed oxygen. The membrane-based fed-batch shake flask in combination with the RAMOS device is a powerful combination to investigate the effect of substrate-limited fed-batch conditions. 相似文献
9.
Distribution and properties of arginase in the salivary glands of four species of laboratory mammals
Yasuda N Moriwaki K Furuyama S 《Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology》2004,174(3):237-242
Important progress in arginine metabolism includes the discovery of widespread expression of two isoforms of arginase, arginase I and II, not only in hepatic cells but also in non-hepatic cells, and the formation of nitric oxide, a widely distributed signal-transducing molecule, from arginine by nitric oxide synthase. Possible physiological roles of arginase may therefore include regulation of nitric oxide synthesis through arginine availability for nitric oxide synthase. In this paper, arginase was investigated in the submandibular, sublingual, and parotid glands of rat, mouse, guinea pig, and rabbit. From their arginase contents, the salivary glands of these species were divided into two groups. Variable levels of arginase activity were detected in the salivary glands of mouse and rat. However, salivary glands of rabbit and guinea pig had almost no arginase activity. The presence of nitric oxide synthase has been reported in all the salivary glands used in this study. Therefore, one of the important findings was the presence of species specificity in the co-localization of arginase and nitric oxide synthase in the salivary glands of the four species. The highest specific activity of arginase was found in mouse parotid gland. In rat, considerable arginase activity was detected in all three glands, at 3.6–7.3% of that in rat liver. In rat submandibular gland, arginase was detected in both cytosolic and particulate fractions. In addition, arginase was detected in isolated acinar cells, but not in duct cells. Experiments on the intracellular distribution and the effects of the arginase inhibitors ornithine and N-hydroxy-L-arginine (NOHA), suggested the presence of both arginase I and arginase II in rat submandibular gland.Abbreviations
cGMP
cyclic guanosine 3,5-monophosphate
-
NO
nitric oxide
-
NOHA
N-hydroxy-L-arginine
-
NOS
nitric oxide synthase
Communicated by I.D. Hume 相似文献
10.
11.
Specific induction of catabolism and its relation to repression of biosynthesis in arginine metabolism of Saccharomyces cerevisiae. 总被引:10,自引:0,他引:10
Experimental results are presented in support of the model previously proposed for specific induction of the synthesis of enzymes for arginine catabolism in Saccharomyces cerevisiae (Wiame, 1971a,b), and its connection with end-product repression of arginine biosynthetic enzymes. The data support the occurrence of negative regulation of metabolism in a eukaryote.Operator regions, one for arginase and another for ornithine transaminase, are identified. The operator mutations are fully constitutive. A mutation compatible with the occurrence of a catabolic represser, CARGR, leads to partial pleiotropic constitutivity.The connection between the induction process and the repression of biosynthetic enzymes is due to a common receptor of metabolic signals, an ambivalent repressor ARGR endowed with the property of a usual repressor for anabolic enzymes and playing the role of inducer at the level of CARGR; this cascade process simulates a positive control. argR? mutations, by producing defective ARGR, “turn on” anabolic enzyme synthesis and “turn off” the synthesis of catabolic enzymes (Fig. 2). The dual role of ARGR is confirmed by the isolation of a mutation argRIId which, in contrast to the defective properties caused by usual argR? mutations, causes a dominant hyperactivity toward induction of a catabolic enzyme, but retains recessive hypoactivity toward repression of an anabolic enzyme. Such an ambivalent repressor is a function necessary for mutual, balanced exclusion between opposite metabolisms.Many operator constitutive mutations for arginase, cargA+O?, change the level of enzyme to a similar value, thus defining a genetic function. One of these mutations, cargA+Oh, in addition to having unusual genetic behaviour, leads to production of twice as much arginase as cargA+O?. This suggests the existence of another genetic region near the structural gene for this enzyme and an additional regulatory function to be analyzed in a separate paper (Dubois &; Wiame, 1978). 相似文献
12.
Dr. Kevin W. Prudence Anthony Katz J. Ann Sugrue Jennifer A. Thomson 《Current microbiology》1989,18(1):27-31
Bacillus subtilis strain 1A297 was shown to relieve the glucose repression of a clonedB. amyloliquefaciens -amylase gene carried on the hybrid plasmid pVC102 without affecting its temporal activation. However, glucose repression of -amylase occurred when pVC102, was introduced intoB. subtilis strain 1A289. Glucose repression was relieved by -methyl-d-glucoside, an analog of glucose that blocks its uptake. The relief of glucose repression in 1A297 did not act at the level of plasmid copy number. As 1A297 was capable of exerting glucose repression on a homologous chromosomally encoded gene, it is postulated that the putativetrans-acting product involved in glucose repression inB. subtilis (Nicholson and Chambliss, 1986, J. Bacteriol. 165:663–670) is altered in strain 1A297 and does not recognize theB. amyloliquefaciens -amylase gene. 相似文献
13.
Datsenko K. A. Evtushenkov A. N. Sergeev K. V. Dobrynina O. Yu. Bolshakova T. N. 《Russian Journal of Genetics》2002,38(7):754-760
Biochemical consequences of mutational damage to common components of the Erwinia phosphoenolpyruvate-dependent phosphotransferase system (the HPr protein and enzyme I) were studied. The transport of glucose, mannose, fructose, and mannitol inErwinia was shown to require a preliminary induction of proteins of the phosphotransferase system. A drastic decrease in the rate of the transport of these carbohydrates was observed in ptsI and ptsH mutants. A disturbance in the common components suppresses the synthesis of inducible enzymes (-galactosidase, complexes of pectolate lyases and cellulases) and renders it resistant to catabolite repression by glucose, but mutants were shown to retain intracellular cAMP content. Erwinia mutants devoid of common components of the system lack phytopathogenic features. The appearance of an intact ptsI allele in the cell completely repaired pleiotropic disturbances in these mutants. 相似文献
14.
The regulation of enzyme synthesis has changed in Bacillus subtilis pleiotropic mutant lacking transketolase (tkt). The tkt mutant is hypersensitive to d-glucose repression of the synthesis of d-mannitol catabolic enzymes, such as d-mannitol-1-phosphate dehydrogenase and d-mannitol transport system. d-Gluconate, d-xylose and l-arabinose are also effectors for repression in the tkt mutant. In contrast, the synthesis of sorbitol catabolic enzymes, such as sorbitol permease and sorbitol dehydrogenase, are almost insensitive to d-glucose repression. These changes in the regulation of enzyme synthesis seem to be related to some defect in the cell surface structure of the tkt mutant by which other pleiotropic properties are also generated. 相似文献
15.
Summary The synthesis of thymine 7-hydroxylase, an -ketoglutarate dependent dioxygenase, is subject both to nitrogen metabolite repression and to oxygen repression, while synthesis of the other pyrimidine salvage pathway dioxygenase, pyrimidine deoxyribonucleoside 2-hydroxylase, is subject to neither. areA300, an allele of the positive acting regulatory gene areA mediating nitrogen metabolite repression in Aspergillus nidulans, considerably elevates levels of thymine 7-hydroxylase, probably alleviating at least partly both nitrogen metabolite repression and oxygen repression. areA300 has little or no effect on levels of pyrimidine deoxyribonucleoside 2-hydroxylase but does elevate net uptake capacities for thymine, thymidine and deoxyuridine two-fold. areA300 was selected as allowing thymine to supplement a pyrimidine auxotrophy and was found to allow supplementation by thymidine, other pyrimidine nucleosides and pyrimidine salvage intermediates as well. This is the first reported evidence for areA control over an activity(-ies) not directly concerned with nitrogen source utilization. 相似文献
16.
The syntheses of arginase and ornithine transaminase were studied in two strains ofSaccharomyces cerevisiae, viz. strain B and strain α-Σ1278b. Derepression of both enzymes during nitrogen starvation was shown only by strain B, non-specific
induction of arginase only by strain α-Σ1278b. This different response of both strains studied reveals substantial differences
in the regulation of enzyme synthesis among yeast strains of one and the same species.
The specific enzyme activities observed in chemostat cultures with arginine as the nitrogen source and different sugars, at
variable carbon to nitrogen ratios, did not indicate the involvement of carbon catabolite repression in the regulation of
arginase and ornithine transaminase syntheses. Specific arginase activities observed in the continuous cultures varied widely
and did not show a correlation with the intracellular arginine concentration. Extracellular steady-state arginine concentrations
higher than about 0.1mm, in addition to abundant energy supply, were found to be required for high production of arginase. It is suggested that,
besides intracellular arginine, extracellular arginine may provide an induction signal necessary for full-scale induction
of arginase synthesis. A possible intermediary role of arginine permeases or of other membrane proteins is discussed. 相似文献
17.
The role of -galactosidase repression in glucose inhibition of lactose utilization was studied inEscherichia coli. Escherichia coli 3300 constitutively produces -galactosidase even in the presence of glucose. When this strain was grown in a mixture of glucose and lactose, lactose utilization did not occur until glucose was depleted. The addition of glucose to a 3300 culture grown in lactose immediately caused a permanent inhibition of lactose utilization and only a mild transient repression of -galactosidase. Exogenous cyclic adenosine monophosphate (AMP) did not overcome the glucose inhibition of lactose utilization but did relieve the transient repression. Thus glucose inhibition of lactose utilization is not related to -galactosidase repression and is independent of cyclic AMP. 相似文献
18.
Bioluminescence and the synthesis of luciferase inVibrio harveyi growing in a minimal medium are repressible by iron; this is not significantly reversed by cyclic adenosine 3,5-monophosphate (cAMP). Cultures grown with added iron emit less light and possess less luciferase per cell than those grown under conditions of limiting iron; this may have significance in relation to the function of luciferase as an electron carrier. With iron, and with glycerol as the sole carbon and energy source, the addition of glucose causes further repression, both transient and permanent, and this is only partially reversible by cAMP. Without iron, glucose addition results in only a small and transient repression, but this is fully reversible by cAMP. The inability of cAMP to reverse iron-influenced repression may be explained by both a low rate of transport of cAMP into the bacteria and increased intracellular levels of cyclic nucleotide phosphodiesterase. 相似文献
19.
The growth of Hansenula polymorpha and Kloeckera sp. 2201 with a mixture of glucose and methanol (38.8%/61.2%, w/w) and the regulation of the methanol dissimilating enzymes alcohol oxidase, catalase, formaldehyde dehydrogenase and formate dehydrogenase were studied in chemostat culture, as a function of the dilution rate. Both organisms utilized and assimilated glucose and methanol simultaneously up to dilution rates of 0.30 h-1 (H. polymorpha) and 0.26h-1, respectively (Kloeckera sp. 2201) which significantly exceeded max found for the two yeasts with methanol as the only source of carbon. At higher dilution rates methanol utilisation ceased and only glucose was assimilated. Over the whole range of mixed-substrate growth both carbon sources were assimilated with the same efficiency as during growth with glucose or methanol alone.In cultures of H. polymorpha, however, the growth yield for glucose was lowered by the unmetabolized methanol at high dilution rates. During growth on both carbon sources the repression of the synthesis of all catabolic methanol enzymes which is normally caused by glucose was overcome by the inductive effect of the simultaneously fed methanol. In both organisms the synthesis of alcohol oxidase was found to be regulated differently as compared to catalase, formaldehyde and formate dehydrogenase. Whereas increasing repression of the synthesis of alcohol oxidase was found with increasing dilution rates as indicated by gradually decreasing specific activities of this enzyme in cell-free extracts, the specific activities of this enzyme in cell-free extracts, the specific activities of catalase and the dehydrogenases increased with increasing growth rates until repression started. The results indicate similar patterns of the regulation of the synthesis of methanol dissimilating enzymes in different methylotrophic yeasts.Abbreviations and Terms C1
Methanol
- C6
glucose; D dilution rate (h-1)
-
D
c
critical dilution rate (h-1)
-
q
s
specific, rate of substrate consumption (g substrate [g cell dry weight]-1 h-1)
-
q
CO2 and q
O2
are the specific rates of carbon dioxide release and oxygen consumption (mmol [g cell dry weight]-1 h-1)
- RQ
respiration quotient (q
CO2
q
O2
1
)
-
s
0(C1) and s
0(C6)
are the concentrations of methanol and glucose in the inflowing medium (g l-1)
-
s
residual substrate concentration in the culture liquid (g l-1)
- Sp. A.
enzyme specific activity
- x
cell dry weight concentration (gl-1)
-
Y
X/C6
growth yield on glucose (g cell dry weight [g substrate]-1 相似文献
20.
Pseudomonas oxalaticus was grown in carbon- and energy-limited continuous cultures either with oxalte or formate or with mixtures of these substrates. During growth on the mixtures, simultaneous utilization of the two substrates occurred at all dilution rates tested. Under these conditions oxalate repressed the synthesis of ribulosebisphosphate carboxylase. The degree of this repression was dependent on the dilution rate and the ratio of oxalate and formate in the medium reservoir. At a fixed oxalate/formate ratio repression was greatest at intermediate dilution rates, whereas derepression occurred at both low and high dilution rates. Progressive depression of ribulosebisphosphate carboxylase synthesis and of autotrophic CO2 fixation at low dilution rates was attributed to the decreasing concentration of intracellular repressor molecule(s), parallel to the decreasing concentration of the growth-limiting substrates in the culture. To account for the derepression at higher dilution rates, it is proposed that the rate of oxalyl-CoA production from oxalate limits the supply of metabolic intermediates and that additional energy and reducing power generated from formate drains the pools of metabolic intermediates sufficiently to lower the intracellular concentration of the repressor(s). During growth of Pseudomonas oxalaticus on the heterotrophic substrate oxalate alone, at dilution rates below 10% of the maximum specific growth rate, derepression of ribulosebisphosphate carboxylase synthesis and of autotrophic CO2 fixation was observed to a level which was 50% of that observed during growth on formate alone at the same dilution rate. It is concluded that in Pseudomonas oxalaticus the synthesis of enzymes involved in autotrophic CO2 fixation via the Calvin cycle is regulated by a repression/derepression mechanism and that the contribution of autotrophic CO2 fixation to the biosynthesis of cell material in this organism is mainly controlled via the synthesis of these enzymes.Abbreviations RuBPCase
ribulosebisphosphate carboxylase
- PMS
phenazine methosulphate
- DCPIP
2,6-dichlorophenolindophenol
- FDH
formate dehydrogenase
- SR
concentration of growth-limiting substrate in reservoir 相似文献