scholarly journals Link between Phosphate Starvation and Glycogen Metabolism in Corynebacterium glutamicum, Revealed by Metabolomics

2010 ◽  
Vol 76 (20) ◽  
pp. 6910-6919 ◽  
Author(s):  
Han Min Woo ◽  
Stephan Noack ◽  
Gerd M. Seibold ◽  
Sabine Willbold ◽  
Bernhard J. Eikmanns ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Corynebacterium Glutamicum ◽  
Carbon Flux ◽  
Glycogen Content ◽  
Glycogen Synthesis ◽  
Glycogen Metabolism ◽  
Metabolite Analysis ◽  
Glycogen Level ◽  
Flux Balance ◽  
Balance Analysis

ABSTRACT In this study, we analyzed the influence of phosphate (Pi) limitation on the metabolism of Corynebacterium glutamicum. Metabolite analysis by gas chromatography-time-of-flight (GC-TOF) mass spectrometry of cells cultivated in glucose minimal medium revealed a greatly increased maltose level under Pi limitation. As maltose formation could be linked to glycogen metabolism, the cellular glycogen content was determined. Unlike in cells grown under Pi excess, the glycogen level in Pi-limited cells remained high in the stationary phase. Surprisingly, even acetate-grown cells, which do not form glycogen under Pi excess, did so under Pi limitation and also retained it in stationary phase. Expression of pgm and glgC, encoding the first two enzymes of glycogen synthesis, phosphoglucomutase and ADP-glucose pyrophosphorylase, was found to be increased 6- and 3-fold under Pi limitation, respectively. Increased glycogen synthesis together with a decreased glycogen degradation might be responsible for the altered glycogen metabolism. Independent from these experimental results, flux balance analysis suggested that an increased carbon flux to glycogen is a solution for C. glutamicum to adapt carbon metabolism to limited Pi concentrations.

scholarly journals The α-Glucan Phosphorylase MalP of Corynebacterium glutamicum Is Subject to Transcriptional Regulation and Competitive Inhibition by ADP-Glucose

2015 ◽  
Vol 197 (8) ◽  
pp. 1394-1407 ◽  
Author(s):  
Lina Clermont ◽  
Arthur Macha ◽  
Laura M. Müller ◽  
Sami M. Derya ◽  
Philipp von Zaluskowski ◽  
...  
Keyword(s):  
Carbon Source ◽  
Corynebacterium Glutamicum ◽  
Glycogen Content ◽  
Current System ◽  
Glycogen Synthesis ◽  
Typical Feature ◽  
Content Type ◽  
Maltose Metabolism ◽  
Glucan Phosphorylase

ABSTRACTα-Glucan phosphorylases contribute to degradation of glycogen and maltodextrins formed in the course of maltose metabolism in bacteria. Accordingly, bacterial α-glucan phosphorylases are classified as either glycogen or maltodextrin phosphorylase, GlgP or MalP, respectively. GlgP and MalP enzymes follow the same catalytic mechanism, and thus their substrate spectra overlap; however, they differ in their regulation: GlgP genes are constitutively expressed and the enzymes are controlled on the activity level, whereas expression of MalP genes are transcriptionally controlled in response to the carbon source used for cultivation. We characterize here the modes of control of the α-glucan phosphorylase MalP of the Gram-positiveCorynebacterium glutamicum. In accordance to the proposed function of themalPgene product as MalP, we found transcription ofmalPto be regulated in response to the carbon source. Moreover,malPtranscription is shown to depend on the growth phase and to occur independently of the cell glycogen content. Surprisingly, we also found MalP activity to be tightly regulated competitively by the presence of ADP-glucose, an intermediate of glycogen synthesis. Since the latter is considered a typical feature of GlgPs, we propose thatC. glutamicumMalP acts as both maltodextrin and glycogen phosphorylase and, based on these findings, we question the current system for classification of bacterial α-glucan phosphorylases.IMPORTANCEBacterial α-glucan phosphorylases have been classified conferring to their purpose as either glycogen or maltodextrin phosphorylases. We found transcription ofmalPinC. glutamicumto be regulated in response to the carbon source, which is recognized as typical for maltodextrin phosphorylases. Surprisingly, we also found MalP activity to be tightly regulated competitively by the presence of ADP-glucose, an intermediate of glycogen synthesis. The latter is considered a typical feature of GlgPs. These findings, taken together, suggest thatC. glutamicumMalP is the first α-glucan phosphorylase that does not fit into the current system for classification of bacterial α-glucan phosphorylases and exemplifies the complex mechanisms underlying the control of glycogen content and maltose metabolism in this model organism.

Effect of hypercorticism on regulation of skeletal muscle glycogen metabolism by insulin

1992 ◽  
Vol 262 (4) ◽  
pp. E427-E433 ◽  
Author(s):  
L. Coderre ◽  
A. K. Srivastava ◽  
J. L. Chiasson
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Content ◽  
Activity Ratio ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Glycogen Metabolism ◽  
Dexamethasone Treatment ◽  
Muscle Glycogen Content ◽  
Glycogen Synthase Activity ◽  
Muscle Glycogen Concentration

The effects of hypercorticism on the regulation of glycogen metabolism by insulin in skeletal muscles was examined by using the hindlimb perfusion technique. Rats were injected daily with either saline or dexamethasone (0.4 mg.kg-1.day-1) for 14 days and were studied in the fed or fasted (24 h) state under saline or insulin (1 mU/ml) treatment. In fed controls, insulin resulted in glycogen synthase activation and in enhanced glycogen synthesis. In dexamethasone-treated animals, basal muscle glycogen concentration remained normal, but glycogen synthase activity ratio was decreased in white and red gastrocnemius and plantaris muscles. Furthermore, insulin failed to activate glycogen synthase and glycogen synthesis. In the controls, fasting was associated with decreased glycogen concentrations and with increased glycogen synthase activity ratio in all four groups of muscles (P less than 0.01). Dexamethasone treatment, however, completely abolished the decrease in muscle glycogen content as well as the augmented glycogen synthase activity ratio associated with fasting. Insulin infusion stimulated glycogen synthesis in fasted controls but not in dexamethasone-treated rats. These data therefore indicate that dexamethasone treatment inhibits the stimulatory effect of insulin on glycogen synthase activity and on glycogen synthesis. Furthermore, hypercorticism suppresses the decrease in muscle glycogen content associated with fasting.

scholarly journals The transcriptional regulators RamA and RamB are involved in the regulation of glycogen synthesis in Corynebacterium glutamicum

Microbiology ◽  
2010 ◽  
Vol 156 (4) ◽  
pp. 1256-1263 ◽  
Author(s):  
Gerd M. Seibold ◽  
Christian T. Hagmann ◽  
Melanie Schietzel ◽  
Denise Emer ◽  
Marc Auchter ◽  
...  
Keyword(s):  
Carbon Source ◽  
Corynebacterium Glutamicum ◽  
Transcriptional Control ◽  
Glycogen Content ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Dry Weight ◽  
Transcriptional Regulators ◽  
Negative Regulator

When grown in glucose-, fructose- or sucrose-containing medium, the amino acid producer Corynebacterium glutamicum transiently accumulates large amounts of glycogen (up to 10 % of its dry weight), whereas only a marginal amount of glycogen is formed during growth with acetate. This carbon-source-dependent regulation is at least partially due to transcriptional control of glgC, encoding ADP-glucose pyrophosphorylase, the first enzyme of glycogen synthesis from glucose-1-phosphate. Here, we have analysed a possible regulatory role for the transcriptional regulators RamA and RamB on glycogen content of the cells and on control of expression of glgC and of glgA, which encodes the second enzyme of glycogen synthesis, glycogen synthase. Determination of the glycogen content of RamA- and RamB-deficient C. glutamicum indicated that RamA and RamB influence glycogen synthesis positively and negatively, respectively. In accordance with the identification of putative RamA and RamB binding sites upstream of glgC and glgA, both regulators were found to bind specifically to the glgC–glgA intergenic promoter region. Promoter activity assays in wild-type and RamA- and RamB-deficient strains of C. glutamicum revealed that (i) RamA is a positive regulator of glgC and glgA, (ii) RamB is a negative regulator of glgA and (iii) neither RamA nor RamB alone is responsible for the carbon-source-dependent regulation of glycogen synthesis in C. glutamicum.

relA Gene control of bacterial glycogen synthesis

1978 ◽  
Vol 56 (6) ◽  
pp. 403-406 ◽  
Author(s):  
William A. Bridger ◽  
William Paranchych
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Stationary Phase ◽  
Nutrient Availability ◽  
Glycogen Content ◽  
Glycogen Synthesis ◽  
Gene Control ◽  
E Coli ◽  
Stimulation Of ◽  
In Cells

Starvation of Escherichia coli K12 for an amino acid results in the stimulation of bacterial glycogen synthesis in cells containing the relA+ gene, but not in cells carrying the relA− allele. Similarly, a large difference in glycogen content is demonstrable between relA+ and relA− cells in stationary phase. It is concluded that guanosine 5′,3′-bis(diphosphate) (ppGpp) or some related relA -dependent metabolite is involved in the regulation of bacterial glycogen synthesis. Detection of significant basal levels of glycogen in a relA− strain of E. coli and in unstarved relA+E. coli indicates that relA control is not absolutely required for glycogen synthesis but serves as a signal for modulation in response to nutrient availability.

Hormonal regulation of glycogen metabolism in white muscle slices from rainbow trout (Oncorhynchus mykiss Walbaum)

2004 ◽  
Vol 287 (6) ◽  
pp. R1344-R1353 ◽  
Author(s):  
Jason Frolow ◽  
C. Louise Milligan
Keyword(s):  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
Muscle Glycogen ◽  
Hormonal Regulation ◽  
White Muscle ◽  
Glycogen Content ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Glycogen Metabolism ◽  
Rainbow Trout Oncorhynchus Mykiss

To test the hypothesis that cortisol and epinephrine have direct regulatory roles in muscle glycogen metabolism and to determine what those roles might be, we developed an in vitro white muscle slice preparation from rainbow trout ( Oncorhynchus mykiss Walbaum). In the absence of hormones, glycogen-depleted muscle slices obtained from exercised trout were capable of significant glycogen synthesis, and the amount of glycogen synthesized was inversely correlated with the initial postexercise glycogen content. When postexercise glycogen levels were <5 μmol/g, about 4.3 μmol/g of glycogen were synthesized, but when postexercise glycogen levels were >5 μmol/g, only about 1.7 μmol/g of glycogen was synthesized. This difference in the amount of glycogen synthesized was reflected in the degree of activation of glycogen synthase. Postexercise glycogen content also influenced the response of the muscle to 10−8 M epinephrine and 10−8 M dexamethasone (a glucocorticoid analog). At high glycogen levels (>5 μmol/g), epinephrine and dexamethasone stimulated glycogen phosphorylase activity and net glycogenolysis, whereas at low (<5 μmol/g) glycogen levels, glycogenesis and activation of glycogen synthase activity prevailed. These data clearly indicate not only is trout muscle capable of in situ glycogenesis, but the amount of glycogen synthesized is a function of initial glycogen content. Furthermore, whereas dexamethasone and epinephrine directly stimulate muscle glycogen metabolism, the net effect is dependent on initial glycogen content.

Flux balance analysis of Corynebacterium glutamicum using a genome-scale metabolic model

2009 ◽  
Vol 108 ◽  
pp. S166
Author(s):  
Chikara Furusawa ◽  
Yohei Shinfuku ◽  
Natee Sorpitiporn ◽  
Masahiro Sono ◽  
Takashi Hirasawa ◽  
...  
Keyword(s):  
Corynebacterium Glutamicum ◽  
Flux Balance Analysis ◽  
Metabolic Model ◽  
Flux Balance ◽  
A Genome ◽  
Balance Analysis ◽  
Genome Scale

scholarly journals Glycogen metabolism in the liver of the developing rat

1976 ◽  
Vol 160 (2) ◽  
pp. 263-270 ◽  
Author(s):  
C Watts ◽  
E R Gain
Keyword(s):  
Glycogen Content ◽  
Glycogen Synthesis ◽  
Active Form ◽  
Fold Increase ◽  
Glycogen Metabolism ◽  
Total Activity ◽  
Similar Amount ◽  
Lag Period ◽  
Glycogen Deposition ◽  
Developing Rat

1. The total activity of glycogen synthease increased 20-fold from day 17 of gestation to birth at day 22, with a further increase of 18% in the 24h after birth. Active synthase (I) rose 45-fold to a maximum at day 21, fell 40% before birth, and then increased by a similar amount 24h after birth. The fraction of synthase in the active form correlated very well with the deposition of glycogen in the liver. 2. Total phosphorylase had a similar developmental pattern of total synthease with an 18-fold increase from day 17 to day 22. The appearance of active phosphorylase showed a lag-period compared with total phosphorylase and did not increase significantly until day 20. The fraction of phosphorylase in the active form did not correlate at all with glycogen deposition or mobilization. 3. There was a close relationshp between the ratio of phosphorylase a/synthase I and the glycogen content of the liver. An increase or decrease in this ratio would result in glycogenolysis of glycogenesis respectively. 4. It is postulated that a cycle between the two enzymes under basal conditions could exist which permits a continuous turnover of glycogen. Such a system would explain why active phosphorylase is always seen, even under conditions of net glycogen synthesis. The differences in hormone sensitivity of synthase and phosphorylase would also be accounted for as only one enzyme would have to respond acutely to hormonal influences.

Synthesis and degradation of glycogen by Schistosoma mansoni worms in vitro

Parasitology ◽  
1989 ◽  
Vol 98 (1) ◽  
pp. 67-73 ◽  
Author(s):  
A. G. M. Tielens ◽  
C. Celik ◽  
J. M. Van Den Heuvel ◽  
R. H. Elfring ◽  
S. G. Van Den Bergh
Keyword(s):  
Schistosoma Mansoni ◽  
Glycogen Content ◽  
Glycogen Synthesis ◽  
Krebs Cycle ◽  
Glycogen Metabolism ◽  
Mammalian Host ◽  
Initial Reduction ◽  
Glycogen Stores ◽  
Synthesis And Degradation

SummaryThe glycogen stores of adult Schistosoma mansoni worms could be labelled by incubation of the worms, after an initial reduction of their glycogen content, in the presence of [6-14C]glucose. Subsequent breakdown of the labelled glycogen by the parasite revealed that glycogen was degraded to lactate and carbon dioxide. The degradation of glycogen, as compared to that of glucose, resulted in slightly different ratios of these two end-products. This indicates that glycogen breakdown did not replace glucose breakdown to the same extent in all cells and that Krebs-cycle activity was not uniformly distributed throughout the cells of this parasite. Both fructose and mannose could replace glucose as an energy source and the rate of glycogen synthesis from either of these two carbohydrates was higher than from glucose. No indications for glyconeogenesis from C3-units were found. Glycogen metabolism of S. mansoni was not influenced by hormones of the mammalian host. It is regulated by the external glucose concentration and by the level of the endogenous glycogen stores. Studies on paired and unpaired worms showed that no interaction between male and female was necessary for the synthesis of glycogen by female worms.

scholarly journals The effects of starvation and re-feeding on glycogen metabolism in mouse tail skin

1983 ◽  
Vol 212 (3) ◽  
pp. 679-683 ◽  
Author(s):  
C S Harmon ◽  
P J R Phizackerley
Keyword(s):  
Glycogen Content ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Glycogen Metabolism ◽  
Access To Food

Although the glycogen content of mouse tail skin was decreased during starvation and was restored on re feeding, the proportion of glycogen synthase in the I form remained constant throughout at about 10% of the total. During the phase of net glycogen synthesis 1.5h after access to food was restored, the concentration of UDP glucose was markedly increased and the proportion of phosphorylase in the a form was significantly decreased.

scholarly journals Glycogen synthetase and the control of glycogen synthesis in the cellular slime mould Dictyostelium discoideum during the growth (myxamoebal) phase

1972 ◽  
Vol 126 (3) ◽  
pp. 617-626 ◽  
Author(s):  
G. Weeks ◽  
J. M. Ashworth
Keyword(s):  
Stationary Phase ◽  
Dictyostelium Discoideum ◽  
Glycogen Content ◽  
Glycogen Synthesis ◽  
Axenic Medium ◽  
Glycogen Accumulation ◽  
Cellular Slime Mould ◽  
Slime Mould ◽  
Glycogen Synthetase ◽  
Cellular Slime

1. Myxamoebae of the cellular slime mould Dictyostelium discoideum Ax-2 that are grown in axenic medium containing 86mm-glucose have seven times the glycogen content of the same myxamoebae grown in the same medium but lacking added carbohydrate. 2. During the transition from the exponential to the stationary phase of growth in axenic medium containing glucose myxamoebae preferentially synthesize glycogen and can have as much as three times the glycogen content during the stationary phase as they have during the exponential phase of growth. 3. The rate of glycogen degradation by myxamoebae is, under all conditions of growth, small compared with the rate of glycogen accumulation and the changes in glycogen content thus reflect altered rates of glycogen synthesis. 4. There is no correlation between the rate of glycogen synthesis by myxamoebae and the glycogen synthetase content of the myxamoebae. 5. The activity of glycogen synthetase of D. discoideum is inhibited by a physiological concentration of ATP and this inhibition is overcome by glucose 6-phosphate. Both effects are especially marked at physiological concentrations of UDP-glucose. 6. The rate of glycogen accumulation by myxamoebae growing exponentially in axenic media can be satisfactorily accounted for in terms of the known intracellular concentrations of glucose 6-phosphate, UDP-glucose and glycogen synthetase. The rate-limiting factors controlling glycogen synthesis by the myxamoebae are apparently the substrate (UDP-glucose) and effector (glucose 6-phosphate and ATP) concentrations rather than the amount of the enzyme.

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