Polyglucose content in the cell and the rate of glucose consumption during synchronous growth of Escherichia coli

Planutis, Kestutis; Planutiene, M.V.; Lazareva, A. V.; Sel'kov, E.E.; Evtodienko, Yu. V.

doi:10.1016/0006-291x(82)91761-2

Cited by 4 publications

(3 citation statements)

References 8 publications

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“…10). Consequently, effective recovery from the stationary phase of growth may be enhanced by the energy derived from the utilization of stored glycogen (48).…”

Section: Figmentioning

confidence: 99%

High Affinity Binding and Allosteric Regulation ofEscherichia coli Glycogen Phosphorylase by the Histidine Phosphocarrier Protein, HPr

Seok

Sondej

Badawi

et al. 1997

Journal of Biological Chemistry

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The histidine phosphocarrier protein (HPr) is an essential element in sugar transport by the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Ligand fishing, using surface plasmon resonance, was used to show the binding of HPr to a nonphosphotransferase protein in extracts of Escherichia coli; the protein was subsequently identified as glycogen phosphorylase (GP). The high affinity (association constant ϳ10 M ؊1), species-specific interaction was also demonstrated in electrophoretic mobility shift experiments by polyacrylamide gel electrophoresis. Equilibrium ultracentrifugation analysis indicates that HPr allosterically regulates the oligomeric state of glycogen phosphorylase. HPr binding increases GP activity to 250% of the level in control assays. Kinetic analysis of coupled enzyme assays shows that the binding of HPr to GP causes a decrease in the K m for glycogen and an increase in the V max for phosphate, indicating a mixed type activation. The stimulatory effect of E. coli HPr on E. coli GP activity is species-specific, and the unphosphorylated form of HPr activates GP more than does the phosphorylated form. Replacement of specific amino acids in HPr results in reduced GP activation; HPr residues Arg-17, Lys-24, Lys-27, Lys-40, Ser-46, Gln-51, and Lys-72 were established to be important. This novel mechanism for the regulation of GP provides the first evidence directly linking E. coli HPr to the regulation of carbohydrate metabolism.

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“…10). Consequently, effective recovery from the stationary phase of growth may be enhanced by the energy derived from the utilization of stored glycogen (48).…”

Section: Figmentioning

confidence: 99%

High Affinity Binding and Allosteric Regulation ofEscherichia coli Glycogen Phosphorylase by the Histidine Phosphocarrier Protein, HPr

Seok

Sondej

Badawi

et al. 1997

Journal of Biological Chemistry

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“…This might be in the form of physical inhibition of cell division through the presence of glycogen granules at putative division sites, or through an alteration in the polymer structure leading to decreased G1P release [37] resulting in less intracellular ATP. It has been shown previously that E. coli cells rely on glycogen breakdown for energy production during cell division as glucose uptake ceases at this stage [15].…”

Section: Discussionmentioning

confidence: 87%

“…This polyglucan consists of short α-1,4 linked glucan chains joined by α-1,6 branchpoints. Three enzymes are known to be involved in its catabolism in the cytosol of E. coli and endogenous glycogen turnover has previously been linked to cell division [15]. It is initially degraded by glycogen phosphorylase (GlgP) [16] that removes external glucose moieties, synthesising glucose 1-phosphate (G1P).…”

Section: Introductionmentioning

confidence: 99%

Disruption of Glycogen Metabolism Alters Cell Size in Escherichia Coli

Walt

Bürgy

Engelbrecht

et al. 2021

Preprint

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Background: The availability of nutrients impacts cell size and growth rate in many organisms. Research in E. coli has traditionally focused on the influence of exogenous nutrient sources on cell size through their effect on growth and cell cycle progression. Utilising a set of mutants where three genes involved in glycogen degradation - glycogen phosphorylase (glgP), glycogen debranching enzyme (glgX) and maltodextrin phosphorylase (malP) - were disrupted, we examined if degradation of this energy storage compound affects cell size. Results: It was found that mutations to malP increased cell lengths and resulted in substantial heterogeneity of cell size. This was most apparent during exponential growth and the phenotype was unaccompanied by alterations in Z-ring occurrence, cellular FtsZ levels and generation times. ∆malP mutant cells did, however, show abnormal nuclear staining patterns and accumulate increased DnaA amounts at late growth stages, indicating a potential effect on DNA replication. Conclusion: This study reveals a link between glycogen metabolism and cell size in E. coli. A disrupted malP allele is associated with cell size heterogeneity and elongation at all stages of growth, without detectable changes to mass doubling time, FtsZ protein levels or division ring frequency.

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An apparatus for the continuous and simultaneous monitoring of oxygen and solute uptake by growing microbial cultures

Misri

Poole

1983

Journal of Microbiological Methods

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Polyglucose content in the cell and the rate of glucose consumption during synchronous growth of Escherichia coli

Cited by 4 publications

References 8 publications

High Affinity Binding and Allosteric Regulation ofEscherichia coli Glycogen Phosphorylase by the Histidine Phosphocarrier Protein, HPr

High Affinity Binding and Allosteric Regulation ofEscherichia coli Glycogen Phosphorylase by the Histidine Phosphocarrier Protein, HPr

Disruption of Glycogen Metabolism Alters Cell Size in Escherichia Coli

An apparatus for the continuous and simultaneous monitoring of oxygen and solute uptake by growing microbial cultures

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