Biosynthesis of bacterial glycogen IX: Regulatory properties of the adenosine diphosphate glucose pyrophosphorylases of the Enterobocteriaceae

Ribéreau-Gayon, G.; Sabraw, Annemiek; Lammel, Claudia J.; Preiss, Jack

doi:10.1016/0003-9861(71)90534-0

Cited by 28 publications

(26 citation statements)

References 27 publications

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“…A solution containing AMP 1 mM and fructose 1,6-diphosphate 0.25 mM was used to inhibit glycogen synthesis [14,16]. A reduction in bio¢lm formation was observed when stationary-phase cells were incubated with the inhibitors (2+ vs. 1+); in contrast, this did not inhibit the capacity of exponential-phase cells to form a bio¢lm (3+ vs. 3+).…”

Section: Inhibition Of Glycogen Synthesismentioning

confidence: 99%

“…The inhibitor adenosine monophosphate (AMP, 1 mM) and an unsaturating concentration of the activator (0.25 mM fructose 1,6-diphosphate), which enhances the inhibitory e¡ect of the AMP [14], were added to the TSB culture medium. S. enteritidis SE3934 was incubated in this medium until it reached the exponential and stationary phases.…”

Section: Inhibition Of Glycogen Synthesismentioning

confidence: 99%

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The relationship between glycogen synthesis, biofilm formation and virulence in Salmonella enteritidis

Bonafonte¹

2000

FEMS Microbiology Letters

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Salmonella enteritidis accumulated large quantities of intracellular polysaccharide when grown in unrestricted nutrient conditions. Dense, abundant cytoplasmic granules were observed by electron microscopy in sections stained by the periodic acid-chlorite technique, indicating that the polysaccharide was of the glycogen type. When biofilm-producing S. enteritidis was pre-incubated in media containing increasing levels of glucose concentration, the levels of both cytoplasmic glycogen and biofilm rose correlatively to a point where a ceiling effect was observed. Studies carried out with activators and inhibitors of glycogen biosynthesis confirmed that biofilm was formed from glycogen cell stores. On the other hand, the virulence of the biofilm-producing strain in infected chickens increased proportionally to the amount of stored glycogen, suggesting a possible role of the glycogen depot in the virulence of S. enteritidis. ß

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Section: Inhibition Of Glycogen Synthesismentioning

confidence: 99%

Section: Inhibition Of Glycogen Synthesismentioning

confidence: 99%

The relationship between glycogen synthesis, biofilm formation and virulence in Salmonella enteritidis

Bonafonte¹

2000

FEMS Microbiology Letters

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“…The physical size of the gigA structural gene is about 1.3 kilobase pairs and has the coding capacity for a protein of 50,000 daltons. This suggests that the subunit molecular ADPglucose pyrophosphorylase from S. typhimurium JP102 has been shown to behave kinetically and immunologically the same as the enzyme fromn S. typhimurium LT2 (17,31,33). We have partially purified ADPglucose pyrophosphorylase from S. typhimurium JP102, a derepressed mutant of ADPglucose pyrophosphorylase and compared it with the same enzyme from E. coli K-12 G6MD3(pPL301).…”

Section: Discussionmentioning

confidence: 88%

“…As might be expected, the ADPglucose pyrophosphorylase of Salmonella typhimurium shows the same spectrum of allosteric activators and inhibitors as the E. coli ADPglucose pyrophosphorylase (31). Therefore, it was of interest to clone the glycogen biosynthetic genes from S. typhimurium, since it may provide more insight in understanding how ADPglucose pyrophosphorylase is allosterically regulated at a structure-function level.…”

mentioning

confidence: 94%

Cloning of the ADPglucose pyrophosphorylase (glgC) and glycogen synthase (glgA) structural genes from Salmonella typhimurium LT2

Leung¹,

Preiss²

1987

J Bacteriol

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The structural genes of ADPglucose pyrophosphorylase (glgC) and glycogen synthase (glgA) from Salmonella typhimurium LT2 were cloned on a 5.8-kilobase-pair insert in the Sail site of pBR322. A single strand specific radioactive probe containing the N terminus of the Escherichia coli K-12 glgC gene in M13mp8 was used to hybridize against a S. typhimurium genomic library in X1059. DNA from a plaque showing a positive hybridization signal was isolated, subcloned into pBR322, and transformed into E. coli K-12 RR1 and E. coli G6MD3 (a mutant with a deletion of the glg genes). Transformants were stained with iodine for the presence of glycogen. E. coli K-12 RR1 transformants stained dark brown, whereas G6MD3 transformants stained greenish yellow, and they both were shown to contain a 5.8-kilobase-pair insert in the Sall site of pBR322, designated pPL301. Enzyme assays of E. coli K-12 G6MD3 harboring pPL301 restored ADPglucose pyrophosphorylase and glycogen synthase activities. The specific activities of ADPglucose pyrophosphorylase and glycogen synthase in E. coil K-12 RR1(pPL301) were increased 6-to 7-fold and 13-to 15-fold, respectively.Immunological and kinetic studies showed that the expressed ADPglucose pyrophosphorylase activity in transformed E. coli K-12 G6MD3 cells was very similar to that of the wild-type enzyme.The biosynthesis of bacterial glycogen involves three enzymes: ADPglucose pyrophosphorylase (EC 2.7.7.27), glycogen synthase (EC 2.4.1.21), and branching enzyme (EC 2.4.1.18), which are encoded by glgC, -A, and -B genes, respectively, in Escherichia coli (12,(27)(28)(29)(30). In this biosynthetic pathway, allosteric regulation has been shown to occur at the ADPglucose pyrophosphorylase level (12,(27)(28)(29)(30). ADPglucose pyrophosphorylase has been isolated and characterized from a number of bacteria, and the nature of the activator has been shown to be related to the major route of carbon metabolism of the particular organism (12,(27)(28)(29)(30).Among the enteric bacteria, ADPglucose pyrophosphorylase is activated by fructose 1,6-bisphosphate (27), whereas ADP, AMP, and Pi are allosteric inhibitors (29, 30).Okita et al. (25) have cloned the gigA, -B, and -C genes from E. coli K-12 into the PstI site of pBR322. The nucleotide sequence of the structural genes glgA, -B, and -C have been reported (2, 3, 13). The allosteric properties of ADPglucose pyrophosphorylase from E. coli K-12 were also studied in great detail with respect to its activator binding site, inhibitor binding site, and substrate binding site (14, 16) by means of a photoaffinity labeling technique with azido adenine nucleotides. The combination of nucleotide sequencing and active site labeling has enabled us to determine the location of the activator, inhibitor, and substrate binding sites.As might be expected, the ADPglucose pyrophosphorylase of Salmonella typhimurium shows the same spectrum of allosteric activators and inhibitors as the E. coli ADPglucose pyrophosphorylase (31). Therefore, it was of interest to clone the glycogen b...

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“…frcundii, Salmonella typhimwium, Entcrobactcr cloacae, and ShigcIla dyscnkrzac arc activated by the glycolytic intermediates fructose-P2, 3-Pglycerate, P-enolpyruvate, 2-P-glyceratc, and 3-P-glyceraldehyde (26)(27)(28). Invariably fructose-P2, TPNH, and pyridoxal-P are the most effective activators.…”

Section: A Activator Specificitymentioning

confidence: 99%

Regulation of Adenosine Diphosphate Glucose Pyrophosphorylase

Preiss

1978

Advances in Enzymology - And Related Areas of Molecular Biology

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Biosynthesis of bacterial glycogen IX: Regulatory properties of the adenosine diphosphate glucose pyrophosphorylases of the Enterobocteriaceae

Cited by 28 publications

References 27 publications

The relationship between glycogen synthesis, biofilm formation and virulence in Salmonella enteritidis

The relationship between glycogen synthesis, biofilm formation and virulence in Salmonella enteritidis

Cloning of the ADPglucose pyrophosphorylase (glgC) and glycogen synthase (glgA) structural genes from Salmonella typhimurium LT2

Regulation of Adenosine Diphosphate Glucose Pyrophosphorylase

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