Catabolite repression-resistant mutants of Bacillus subtilis

1979 ◽  
Vol 25 (11) ◽  
pp. 1283-1287 ◽  
Author(s):  
I. Takahashi
Keyword(s):  
Bacillus Subtilis ◽  
Carbon Source ◽  
Catabolite Repression ◽  
Minimal Medium ◽  
Carbon Sources ◽  
Close Relation ◽  
Selection Technique ◽  
Source Studies ◽  
Resistant Mutants ◽  
Simple Selection

Mutants of Bacillus subtilis that are able to sporulate under the condition of catabolite repression were isolated by a simple selection technique. The mutants used in the present study were able to grow normally on minimal medium with ammonium sulphate as the nitrogen source and glucose as the carbon source. Studies carried out with these mutants show that there is no close relation between catabolite repression of an inducible enzyme, acetoin dehydrogenase, and that of sporulation. Certain mutants are able to sporulate in the presence of all the carbon sources tested but some mutants are resistant only to the carbon source used in isolation. It is suggested that several metabolic steps may be affected in catabolite repression of sporulation.

Effect of carbon source on extracellular (1 → 3)- and (1 → 6)-β-glucanase production by Acremonium persicinum

1997 ◽  
Vol 43 (5) ◽  
pp. 432-439 ◽  
Author(s):  
Stuart M. Pitson ◽  
Robert J. Seviour ◽  
Barbara M. McDougall
Keyword(s):  
Carbon Source ◽  
Filamentous Fungus ◽  
Catabolite Repression ◽  
Carbon Catabolite Repression ◽  
Carbon Sources ◽  
Culture Filtrates ◽  
Regulation Of Synthesis

The effect of carbon source on the levels of three (1 → 3)-β-glucanases and a (1 → 6)-β-glucanase in the culture filtrates of the filamentous fungus Acremonium persicinum was investigated. All four enzymes were produced during growth of the fungus on (1 → 3)-, (1 → 6)-, and (1 → 3)(1 → 6)-β-glucans as well as β-linked oligoglucosides. However, only one (1 → 3)-β-glucanase and the (1 → 6)-β-glucanase were detected during growth on a range of other carbon sources including glucose, carboxymethylcellulose, and the α-glucan pullulan. The presence of glucose in the medium markedly decreased the production of all four glucanases, although the concentration required to effect complete repression of enzyme levels varied for the different enzymes. Similar repressive effects were also observed with sucrose, fructose, and galactose. The most likely explanations for these observations are that the synthesis of the (1 → 6)-β-glucanase and one of the (1 → 3)-β-glucanases is controlled by carbon catabolite repression, while the remaining two (1 → 3)-β-glucanases are inducible enzymes subject to carbon catabolite repression.Key words: (1 → 3)-β-glucanase, (1 → 6)-β-glucanase, Acremonium persicinum, regulation of synthesis, fungal β-glucanases.

Relationship between carbon source and susceptibility of Cephalosporium acremonium to selected amino acid analogues

1979 ◽  
Vol 25 (7) ◽  
pp. 818-821 ◽  
Author(s):  
R. J. Mehta ◽  
C. H. Nash
Keyword(s):  
Amino Acid ◽  
Carbon Source ◽  
Carbon Sources ◽  
Soluble Starch ◽  
Cephalosporium Acremonium ◽  
Specific Amino Acid ◽  
Minimal Inhibitory Concentrations ◽  
Amino Acid Analogues ◽  
Resistant Mutants

The susceptibility of Cephalosporium acremonium to selected amino acid analogues was markedly influenced by the carbon source used in the test media. Lysine hydroxamate, β-hydroxy norvaline, and hexafluorovaline were toxic when tested with ribose, ribose or fructose, and ribose or galactose, respectively. In contrast, thialysine and thiaisoleucine inhibited C. acremonium with glucose, fructose, galactose, sucrose, mannitol, sorbitol, and soluble starch. Neither of these analogues was toxic at levels tested when glycerol was used as a carbon source. The minimal inhibitory concentrations (MIC) of thialysine, homoserine, and α-methylserine were > 1000, > 1000, and 250 μg/mL, respectively, with glycerol. In contrast, the MIC values for the same three analogues were 31, 62, and 125 μg/mL, respectively, with mannitol. The matching of the carbon sources with the specific amino acid analogues expands the number of analogues useful for selecting derepressed mutants. Thialysine-resistant mutants (tlysR) of C. acremonium which excrete lysine were isolated on a medium containing mannitol.

Genetic mapping of catabolite-resistant mutants of Bacillus subtilis

1982 ◽  
Vol 28 (11) ◽  
pp. 1242-1251 ◽  
Author(s):  
Dongxu Sun ◽  
I. Takahashi
Keyword(s):  
Bacillus Subtilis ◽  
Genetic Mapping ◽  
Carbon Sources ◽  
Resistance Mutations ◽  
Resistant Mutants ◽  
High Concentrations

Using mutants of Bacillus subtilis that are able to sporulate in the presence of relatively high concentrations of various carbon sources, catabolite resistance mutations were mapped by PBS1 transduction and transformation. Catabolite resistance mutations were localized at six different loci on the chromosome of B. subtilis. The map positions of our mutants suggest that they are distinct from sacUh, catA, and scoC reported by other investigators. Relations between our findings and initiation of sporulation have been discussed.

scholarly journals Catabolite Repression Control of napF (Periplasmic Nitrate Reductase) Operon Expression in Escherichia coli K-12

2008 ◽  
Vol 191 (3) ◽  
pp. 996-1005 ◽  
Author(s):  
Valley Stewart ◽  
Peggy J. Bledsoe ◽  
Li-Ling Chen ◽  
Amie Cai
Keyword(s):  
Escherichia Coli ◽  
Carbon Source ◽  
Nitrate Reductase ◽  
Catabolite Repression ◽  
Carbon Sources ◽  
Anaerobic Growth ◽  
Periplasmic Nitrate Reductase ◽  
Membrane Bound ◽  
Operon Expression ◽  
K 12

ABSTRACT Escherichia coli, a facultative aerobe, expresses two distinct respiratory nitrate reductases. The periplasmic NapABC enzyme likely functions during growth in nitrate-limited environments, whereas the membrane-bound NarGHI enzyme functions during growth in nitrate-rich environments. Maximal expression of the napFDAGHBC operon encoding periplasmic nitrate reductase results from synergistic transcription activation by the Fnr and phospho-NarP proteins, acting in response to anaerobiosis and nitrate or nitrite, respectively. Here, we report that, during anaerobic growth with no added nitrate, less-preferred carbon sources stimulated napF operon expression by as much as fourfold relative to glucose. Deletion analysis identified a cyclic AMP receptor protein (Crp) binding site upstream of the NarP and Fnr sites as being required for this stimulation. The napD and nrfA operon control regions from Shewanella spp. also have apparent Crp and Fnr sites, and expression from the Shewanella oneidensis nrfA control region cloned in E. coli was subject to catabolite repression. In contrast, the carbon source had relatively little effect on expression of the narGHJI operon encoding membrane-bound nitrate reductase under any growth condition tested. Carbon source oxidation state had no influence on synthesis of either nitrate reductase. The results suggest that the Fnr and Crp proteins may act synergistically to enhance NapABC synthesis during growth with poor carbon sources to help obtain energy from low levels of nitrate.

scholarly journals Optimization of Cellulase Production from Bacteria Isolated from Soil

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Sonia Sethi ◽  
Aparna Datta ◽  
B. Lal Gupta ◽  
Saksham Gupta
Keyword(s):  
Bacillus Subtilis ◽  
Carbon Source ◽  
Pseudomonas Fluorescens ◽  
Carbon Sources ◽  
Nitrogen Sources ◽  
Fermentation Medium ◽  
Cellulase Production ◽  
Culture Conditions ◽  
Optimum Conditions ◽  
E Coli

Cellulase-producing bacteria were isolated from soil and identified as Pseudomonas fluorescens, Bacillus subtilIs, E. coli, and Serratia marcescens. Optimization of the fermentation medium for maximum cellulase production was carried out. The culture conditions like pH, temperature, carbon sources, and nitrogen sources were optimized. The optimum conditions found for cellulase production were 40°C at pH 10 with glucose as carbon source and ammonium sulphate as nitrogen source, and coconut cake stimulates the production of cellulase. Among bacteria, Pseudomonas fluorescens is the best cellulase producer among the four followed by Bacillus subtilis, E. coli, and Serratia marscens.

A time resolved metabolomics study: the influence of different carbon sources during growth and starvation of Bacillus subtilis

2014 ◽  
Vol 10 (7) ◽  
pp. 1812-1823 ◽  
Author(s):  
Hanna Meyer ◽  
Hendrikje Weidmann ◽  
Ulrike Mäder ◽  
Michael Hecker ◽  
Uwe Völker ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Carbon Source ◽  
Carbon Sources ◽  
Time Resolved ◽  
Metabolomics Study ◽  
Comprehensive Metabolomics ◽  
Metabolomics Analysis

Bacillus subtilisshows a remarkable robust metabolism towards changing carbon source combinations proved by comprehensive metabolomics analysis.

scholarly journals The Absence of Pyruvate Kinase Affects Glucose-Dependent Carbon Catabolite Repression in Bacillus subtilis

Metabolites ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 216 ◽  
Author(s):  
Sousa ◽  
Westhoff ◽  
Methling ◽  
Lalk
Keyword(s):  
Bacillus Subtilis ◽  
Pyruvate Kinase ◽  
Catabolite Repression ◽  
Carbon Catabolite Repression ◽  
Carbon Sources ◽  
Defined Medium ◽  
Central Carbon Metabolism ◽  
Alternative Pathways ◽  
Distribution Point ◽  
Nutritional Compounds

Pyruvate is a key intermediate of diverse metabolic pathways of central carbon metabolism. In addition to being the end product of glycolysis, pyruvate is an essential carbon distribution point to oxidative metabolism, amino acid and fatty acid syntheses, and overflow metabolite production. Hence, a tight regulation of pyruvate kinase (Pyk) activity is of great importance. This study aimed to analyze targeted metabolites from several pathways and possible changes in Bacillus subtilis lacking Pyk. Wild type and Δpyk cells were cultivated in chemically defined medium with glucose and pyruvate as carbon sources, and the extracted metabolites were analyzed by 1H-NMR, GC-MS, HPLC-MS, and LC-MS/MS. The results showed that the perturbation created in the pyruvate node drove an adaptation to new conditions by altering the nutritional compounds’ consumption. In Δpyk, pyruvate, which is subject to glucose-dependent carbon catabolite repression, did not comply with the hierarchy in carbon source utilization. Other metabolic alterations were observed such as the higher secretion of the overflow metabolites acetoin and 2,3-butanediol by Δpyk. Our results help to elucidate the regulatory transport of glucose and pyruvate in B. subtilis and possible metabolic reroute to alternative pathways in the absence of Pyk.

scholarly journals Carbon Catabolite Repression in Bacillus subtilis: Quantitative Analysis of Repression Exerted by Different Carbon Sources

2008 ◽  
Vol 190 (21) ◽  
pp. 7275-7284 ◽  
Author(s):  
Kalpana D. Singh ◽  
Matthias H. Schmalisch ◽  
Jörg Stülke ◽  
Boris Görke
Keyword(s):  
Bacillus Subtilis ◽  
Catabolite Repression ◽  
Carbon Catabolite Repression ◽  
Carbon Sources ◽  
Transport Activity ◽  
Phosphotransferase System ◽  
Phosphorylation State ◽  
Mechanism Operative

ABSTRACT In many bacteria glucose is the preferred carbon source and represses the utilization of secondary substrates. In Bacillus subtilis, this carbon catabolite repression (CCR) is achieved by the global transcription regulator CcpA, whose activity is triggered by the availability of its phosphorylated cofactors, HPr(Ser46-P) and Crh(Ser46-P). Phosphorylation of these proteins is catalyzed by the metabolite-controlled kinase HPrK/P. Recent studies have focused on glucose as a repressing substrate. Here, we show that many carbohydrates cause CCR. The substrates form a hierarchy in their ability to exert repression via the CcpA-mediated CCR pathway. Of the two cofactors, HPr is sufficient for complete CCR. In contrast, Crh cannot substitute for HPr on substrates that cause a strong repression. Determination of the phosphorylation state of HPr in vivo revealed a correlation between the strength of repression and the degree of phosphorylation of HPr at Ser46. Sugars transported by the phosphotransferase system (PTS) cause the strongest repression. However, the phosphorylation state of HPr at its His15 residue and PTS transport activity have no impact on the global CCR mechanism, which is a major difference compared to the mechanism operative in Escherichia coli. Our data suggest that the hierarchy in CCR exerted by the different substrates is exclusively determined by the activity of HPrK/P.

scholarly journals Control of Inducer Accumulation Plays a Key Role in Succinate-Mediated Catabolite Repression in Sinorhizobiummeliloti

2002 ◽  
Vol 184 (19) ◽  
pp. 5385-5392 ◽  
Author(s):  
Ryan M. Bringhurst ◽  
Daniel J. Gage
Keyword(s):  
Catabolite Repression ◽  
Double Mutant ◽  
Minimal Medium ◽  
Carbon Sources ◽  
Constitutive Expression ◽  
Dicarboxylic Acids ◽  
Genetic Screen ◽  
Aberrant Expression ◽  
Inducer Exclusion ◽  
Secondary Carbon

ABSTRACT The symbiotic, nitrogen-fixing bacterium Sinorhizobium meliloti favors succinate and related dicarboxylic acids as carbon sources. As a preferred carbon source, succinate can exert catabolite repression upon genes needed for the utilization of many secondary carbon sources, including the α-galactosides raffinose and stachyose. We isolated lacR mutants in a genetic screen designed to find S. meliloti mutants that had abnormal succinate-mediated catabolite repression of the melA-agp genes, which are required for the utilization of raffinose and other α-galactosides. The loss of catabolite repression in lacR mutants was seen in cells grown in minimal medium containing succinate and raffinose and grown in succinate and lactose. For succinate and lactose, the loss of catabolite repression could be attributed to the constitutive expression of β-galactoside utilization genes in lacR mutants. However, the inactivation of lacR did not cause the constitutive expression of α-galactoside utilization genes but caused the aberrant expression of these genes only when succinate was present. To explain the loss of diauxie in succinate and raffinose, we propose a model in which lacR mutants overproduce β-galactoside transporters, thereby overwhelming the inducer exclusion mechanisms of succinate-mediated catabolite repression. Thus, some raffinose could be transported by the overproduced β-galactoside transporters and cause the induction of α-galactoside utilization genes in the presence of both succinate and raffinose. This model is supported by the restoration of diauxie in a lacF lacR double mutant (lacF encodes a β-galactoside transport protein) grown in medium containing succinate and raffinose. Biochemical support for the idea that succinate-mediated repression operates by preventing inducer accumulation also comes from uptake assays, which showed that cells grown in raffinose and exposed to succinate have a decreased rate of raffinose transport compared to control cells not exposed to succinate.

scholarly journals Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5

2016 ◽  
Vol 82 (20) ◽  
pp. 6080-6090 ◽  
Author(s):  
Chia-Suei Hung ◽  
Sandra Zingarelli ◽  
Lloyd J. Nadeau ◽  
Justin C. Biffinger ◽  
Carrie A. Drake ◽  
...  
Keyword(s):  
Carbon Source ◽  
Catabolite Repression ◽  
Carbon Catabolite Repression ◽  
Carbon Sources ◽  
Regulatory Elements ◽  
Dependent Manner ◽  
Content Type ◽  
Intergenic Sequences ◽  
Degradation Activity ◽  
The Impact

ABSTRACTPolyester polyurethane (PU) coatings are widely used to help protect underlying structural surfaces but are susceptible to biological degradation. PUs are susceptible to degradation byPseudomonasspecies, due in part to the degradative activity of secreted hydrolytic enzymes. Microorganisms often respond to environmental cues by secreting enzymes or secondary metabolites to benefit their survival. This study investigated the impact of exposing severalPseudomonasstrains to select carbon sources on the degradation of the colloidal polyester polyurethane Impranil DLN (Impranil). The prototypicPseudomonas protegensstrain Pf-5 exhibited Impranil-degrading activities when grown in sodium citrate but not in glucose-containing medium. Glucose also inhibited the induction of Impranil-degrading activity by citrate-fed Pf-5 in a dose-dependent manner. Biochemical and mutational analyses identified two extracellular lipases present in the Pf-5 culture supernatant (PueA and PueB) that were involved in degradation of Impranil. Deletion of thepueAgene reduced Impranil-clearing activities, whilepueBdeletion exhibited little effect. Removal of both genes was necessary to stop degradation of the polyurethane. Bioinformatic analysis showed that putative Cbr/Hfq/Crc-mediated regulatory elements were present in the intergenic sequences upstream of bothpueAandpueBgenes. Our results confirmed that both PueA and PueB extracellular enzymes act in concert to degrade Impranil. Furthermore, our data showed that carbon sources in the growth medium directly affected the levels of Impranil-degrading activity but that carbon source effects varied amongPseudomonasstrains. This study uncovered an intricate and complicated regulation ofP. protegensPU degradation activity controlled by carbon catabolite repression.IMPORTANCEPolyurethane (PU) coatings are commonly used to protect metals from corrosion. Microbiologically induced PU degradation might pose a substantial problem for the integrity of these coatings. Microorganisms from diverse genera, including pseudomonads, possess the ability to degrade PUs via various means. This work identified two extracellular lipases, PueA and PueB, secreted byP. protegensstrain Pf-5, to be responsible for the degradation of a colloidal polyester PU, Impranil. This study also revealed that the expression of the degradative activity by strain Pf-5 is controlled by glucose carbon catabolite repression. Furthermore, this study showed that the Impranil-degrading activity of many otherPseudomonasstrains could be influenced by different carbon sources. This work shed light on the carbon source regulation of PU degradation activity among pseudomonads and identified the polyurethane lipases inP. protegens.

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