Analysis of Sucrose Catabolism in Klebsiella pneumoniae and in Scr+ Derivatives of Escherichia coli K12

Sprenger, Georg A.; Lengeler, Joseph W.

doi:10.1099/00221287-134-6-1635

Cited by 35 publications

(37 citation statements)

References 23 publications

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“…Many bacterial species, including Klebsiella pneumoniae (Sprenger & Lengeler, 1988 ;Titgemeyer et al, 1996), Bacillus subtilis (Fouet et al, 1987), Lactococcus lactis (Thompson & Chassy, 1981 ;Thompson et al, 1991 ;Rauch & deVos, 1992), Fusobacterium mortiferum (Thompson et al, 1992), Escherichia coli (Schmid et al, 1988) and Clostridium beijerinckii (Tangney et al, 1998 ;Reid et al, 1999) with phosphorylation at C-6 of the glucosyl moiety via the phosphoenolpyruvate-dependent sucrose : phosphotransferase system (PEP : PTS) (Meadow et al, 1990 ;Postma et al, 1993). Sucrose 6-phosphate is hydrolysed intracellularly by sucrose-6-phosphate hydrolase (S6PH) to yield glucose 6-phosphate and fructose, which are further metabolized via the glycolytic pathway.…”

Section: Introductionmentioning

confidence: 99%

Metabolism of sucrose and its five isomers by Fusobacterium mortiferum

et al. 2002

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Fusobacterium mortiferum utilizes sucrose [glucose-fructose in α(1 2) linkage] and its five isomeric α-D-glucosyl-D-fructoses as energy sources for growth.Sucrose-grown cells are induced for both sucrose-6-phosphate hydrolase (S6PH) and fructokinase (FK), but the two enzymes are not expressed above constitutive levels during growth on the isomeric compounds. Extracts of cells grown previously on the sucrose isomers trehalulose α(1 1), turanose α(1 3), maltulose α(1 4), leucrose α(1 5) and palatinose α(1 6) contained high levels of an NAD M plus metal-dependent phospho-α-glucosidase (MalH). The latter enzyme was not induced during growth on sucrose. MalH catalysed the hydrolysis of the 6'-phosphorylated derivatives of the five isomers to yield glucose 6-phosphate and fructose, but sucrose 6-phosphate itself was not a substrate. Unexpectedly, MalH hydrolysed both α-and β-linked stereomers of the chromogenic analogue p-nitrophenyl glucoside 6-phosphate. The gene malH is adjacent to malB and malR, which encode an EII(CB) component of the phosphoenolpyruvate-dependent sugar :phosphotransferase system and a putative regulatory protein, respectively. The authors suggest that for F. mortiferum, the products of malB and malH catalyse the phosphorylative translocation and intracellular hydrolysis of the five isomers of sucrose and of related α-linked glucosides. Genes homologous to malB and malH are present in both Klebsiella pneumoniae and the enterohaemorrhagic strain Escherichia coli O157 :H7. Both these organisms grew well on sucrose, but only K. pneumoniae exhibited growth on the isomeric compounds.

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Section: Introductionmentioning

confidence: 99%

Metabolism of sucrose and its five isomers by Fusobacterium mortiferum

et al. 2002

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“…The genes involved in sucrose metabolism of E. amylovora showed significant homology to the scr genes of Salmonella enterica serovar Typhimurium with pUR400 and of K. pneumoniae (45,49). Conserved amino acid motifs in the N terminus of scr proteins of E. amylovora indicated biological function related to the enzymes from pUR400, K. pneumoniae, and other proteins in the family.…”

Section: Discussionmentioning

confidence: 99%

“…In E. coli and Salmonella spp., the conjugative plasmid pUR400 confers the ability to utilize sucrose (54), whereas the scr regulon of K. pneumoniae is located on the chromosome (42, 49). In these bacteria, the uptake of sucrose is mediated via the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system (PTS), yielding sucrose 6-phosphate, which is cleaved by an intracellular hydrolase into glucose 6-phosphate and fructose (45,49). The scr regulons of K. pneumoniae and pUR400 consist of four structural genes: scrK codes for an ATP-dependent fructokinase (5), scrY codes for a sucrose-specific porin of the outer membrane (30), scrA codes for enzyme II scr of the PTS, and scrB codes for an intracellular ␤-D-fructofuranoside fructohydrolase (EC 3.2.1.26), which cleaves sucrose 6-phosphate into ␤-D-fructose and ␣-D-glucose 6-phosphate (51).…”

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confidence: 99%

“…(45,49). In E. coli and Salmonella spp., the conjugative plasmid pUR400 confers the ability to utilize sucrose (54), whereas the scr regulon of K. pneumoniae is located on the chromosome (42,49). In these bacteria, the uptake of sucrose is mediated via the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system (PTS), yielding sucrose 6-phosphate, which is cleaved by an intracellular hydrolase into glucose 6-phosphate and fructose (45,49).…”

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Molecular Analysis of Sucrose Metabolism of Erwinia amylovora and Influence on Bacterial Virulence

Bogs

Geider

2000

J Bacteriol

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Sucrose is an important storage and transport sugar of plants and an energy source for many phytopathogenic bacteria. To analyze regulation and biochemistry of sucrose metabolism of the fire blight pathogen Erwinia amylovora, a chromosomal fragment which enabled Escherichia coli to utilize sucrose as sole carbon source was cloned. By transposon mutagenesis, the scr regulon of E. amylovora was tagged, and its nucleotide sequence was determined. Five open reading frames, with the genes scrK, scrY, scrA, scrB, and scrR, had high homology to genes of the scr regulons from Klebsiella pneumoniae and plasmid pUR400. scrB and scrR of E. amylovora were fused to a histidine tag and to the maltose-binding protein (MalE) of E. coli, respectively. ScrB (53 kDa) catalyzed the hydrolysis of sucrose with a K m of 125 mM. Binding of a MalE-ScrR fusion protein to an scrYAB promoter fragment was shown by gel mobility shifts. This complex dissociated in the presence of fructose but not after addition of sucrose. Expression of the scr regulon was studied with an scrYAB promotergreen fluorescent protein gene fusion and measured by flow cytometry and spectrofluorometry. The operon was affected by catabolite repression and induced by sucrose or fructose. The level of gene induction correlated to the sucrose concentration in plant tissue, as shown by flow cytometry. Sucrose mutants created by site-directed mutagenesis did not produce significant fire blight symptoms on apple seedlings, indicating the importance of sucrose metabolism for colonization of host plants by E. amylovora.The gram-negative bacterium Erwinia amylovora causes fire blight of apple, pear, and other rosaceous plants. Pathogenecity depends on the ability to produce the exopolysaccharide amylovoran (10, 13), to elicit a hypersensitive response on non-host plants (6,8), and to metabolize sorbitol of the host plants (1). Rosaceous plants contain sorbitol and sucrose as storage and transport carbohydrates. The distribution of these carbohydrates is dependent on environmental conditions, species, and plant tissue (28, 52). The highest concentration of sucrose was found in the nectaries of host plants (14), which are assumed to be the main entry site for the pathogen when the pathogen is distributed by insects.Sucrose is utilized by some but not all bacteria extracellularily or intracellularily. E. amylovora can metabolize sucrose via the secreted levansucrase, which polymerizes the homopolysaccharide levan and releases glucose from sucrose (27,29), but also by uptake and intracellular metabolism.The sucrose-utilizing system of enteric bacteria has been studied in Klebsiella pneumoniae and in some isolates of Escherichia coli and Salmonella spp. (45, 49). In E. coli and Salmonella spp., the conjugative plasmid pUR400 confers the ability to utilize sucrose (54), whereas the scr regulon of K. pneumoniae is located on the chromosome (42, 49). In these bacteria, the uptake of sucrose is mediated via the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system (PTS),...

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