UDP-sugar hydrolase isozymes inSalmonella entericaandEscherichia coli: Silent alleles ofushAin related strains of Group ISalmonellaisolates, and ofushBin wild-type and K12 strains ofE. coli, indicate recent and early silencing events, respectively

Edwards, Catherine J.; Innes, David J.; Burns, Dennis M.; Beacham, Ifor R.

doi:10.1111/j.1574-6968.1993.tb06588.x

Cited by 20 publications

(2 citation statements)

References 9 publications

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“…Fourth, TBlastN hits, even with high scores, reveal the presence of the corresponding genes but do not warrant that they are expressed or that the proteins encoded are enzymatically active. In fact, for instance, silent alleles of ushA have been reported in S. enterica and E. coli [ 42 , 43 , 44 , 45 ].…”

Section: Discussionmentioning

confidence: 99%

Genomic Distribution of ushA-like Genes in Bacteria: Comparison to cpdB-like Genes

Ribeiro,

Cameselle

2023

Genes

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UshA and CpdB are nucleotidases of the periplasm of several Gram-negative bacteria, while several Gram-positives contain cell wall-bound variants. UshA is a 5′-nucleotidase, a UDP-sugar hydrolase, and a CDP-alcohol hydrolase. CpdB acts as a 3′-nucleotidase and as a phosphodiesterase of 2′,3′-cyclic nucleotides and 3′,5′-linear and cyclic dinucleotides. Both proteins are pro-virulent for the pathogens producing them and facilitate escape from the innate immunity of the infected host. Recently, the genomic distribution of cpdB-like genes in Bacteria was found to be non-homogeneous among different taxa, and differences occur within single taxa, even at species level. Similitudes and differences between UshA-like and CpdB-like proteins prompted parallel analysis of their genomic distributions in Bacteria. The presence of ushA-like and cpdB-like genes was tested by TBlastN analysis using seven protein probes to query the NCBI Complete Genomes Database. It is concluded that the distribution of ushA-like genes, like that of cpdB-like genes, is non-homogeneous. There is a partial correlation between both gene kinds: in some taxa, both are present or absent, while in others, only one is present. The result is an extensive catalog of the genomic distribution of these genes at different levels, from phylum to species, constituting a starting point for research using other in silico or experimental approaches.

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Section: Discussionmentioning

confidence: 99%

Genomic Distribution of ushA-like Genes in Bacteria: Comparison to cpdB-like Genes

Ribeiro,

Cameselle

2023

Genes

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“…As well as differing in their cellular location, these enzymes display no sequence or antigenic similarities. Interestingly, whilst most S. enterica serotypes contain both activities, most serotype Typhimurium isolates contain an inactive (cryptic) ushA allele [5][6][7]. Likewise, E. coli K-12 and natural isolates of E. coli contain no detectable membrane-associated UDP-glucose hydrolase activity [1] due to an inactive allele of ushB [5,8].…”

Section: Introductionmentioning

confidence: 99%

Bacterial UDP-Glucose Hydrolases and P2 Receptor-Mediated Responses to Infection: A Commentary

Beacham¹,

Headrick²

2013

AID

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UDP-glucose hydrolases are a group of relatively little known membrane-bound or periplasmic enzymes found in Salmonella enterica and E. coli. UDP-glucose is an agonist for a specific P2 receptor (P2Y 14 ) found on epithelial cells and cells associated with innate immunity. It is also recognised as a 'danger signal'. Cells respond to mechanical damage by releasing UDP-glucose which activates P2Y 14 to trigger an innate immune response; it is postulated that a similar response to bacterial infection may be protective against infection. However, the UDP-glucose hydrolases may constitute virulence factors able to abrogate this response by degradation of the released UDP-glucose.

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The role of the intracellular inhibitor of periplasmic UDP-sugar hydrolase (5′-nucleotidase) inEscherichia coli: cytoplasmic localisation of 5′-nucleotidase is conditionally lethal

Innes

Beacham

Burns

2001

J. Basic Microbiol.

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E. coli UshA, a bifunctional enzyme with UDP‐sugar hydrolase and 5′‐nucleotidase activities, is secreted to the periplasm but has a specific protein inhibitor located in the cytoplasm. It has been previously suggested that some 5′‐nucleotidase, or a folded domain of this enzyme, may be active in the cytoplasm prior to export. If true, the intracellular inhibitor may have a role in protecting the cell from the likely deleterious effects of any intracellular UshA activity. Using deletion mutagenesis to remove the UshA signal peptide, we have shown that the resulting UshA derivative is an active cytoplasmic 5′‐nucleotidase, and causes conditional lethality. Our results support the hypothesis that the physiological role of the UshA inhibitor is to protect the intracellular nucleotide pool from any cytoplasmic 5′‐nucleotidase activity.

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UDP-sugar hydrolase isozymes inSalmonella entericaandEscherichia coli: Silent alleles ofushAin related strains of Group ISalmonellaisolates, and ofushBin wild-type and K12 strains ofE. coli, indicate recent and early silencing events, respectively

Cited by 20 publications

References 9 publications

Genomic Distribution of ushA-like Genes in Bacteria: Comparison to cpdB-like Genes

Genomic Distribution of ushA-like Genes in Bacteria: Comparison to cpdB-like Genes

Bacterial UDP-Glucose Hydrolases and P2 Receptor-Mediated Responses to Infection: A Commentary

The role of the intracellular inhibitor of periplasmic UDP-sugar hydrolase (5′-nucleotidase) inEscherichia coli: cytoplasmic localisation of 5′-nucleotidase is conditionally lethal

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