Literature DB >> 28461448

The Response to 2-Aminoacrylate Differs in Escherichia coli and Salmonella enterica, despite Shared Metabolic Components.

Andrew J Borchert1, Diana M Downs2.   

Abstract

The metabolic network of an organism includes the sum total of the biochemical reactions present. In microbes, this network has an impeccable ability to sense and respond to perturbations caused by internal or external stimuli. The metabolic potential (i.e., network structure) of an organism is often drawn from the genome sequence, based on the presence of enzymes deemed to indicate specific pathways. Escherichia coli and Salmonella enterica are members of the Enterobacteriaceae family of Gram-negative bacteria that share the majority of their metabolic components and regulatory machinery as the "core genome." In S. enterica, the ability of the enamine intermediate 2-aminoacrylate (2AA) to inactivate a number of pyridoxal 5'-phosphate (PLP)-dependent enzymes has been established in vivo In this study, 2AA metabolism and the consequences of its accumulation were investigated in E. coli The data showed that despite the conservation of all relevant enzymes, S. enterica and E. coli differed in both the generation and detrimental consequences of 2AA. In total, these findings suggest that the structure of the metabolic network surrounding the generation and response to endogenous 2AA stress differs between S. enterica and E. coliIMPORTANCE This work compared the metabolic networks surrounding the endogenous stressor 2-aminoacrylate in two closely related members of the Enterobacteriaceae The data showed that despite the conservation of all relevant enzymes in this metabolic node, the two closely related organisms diverged in their metabolic network structures. This work highlights how a set of conserved components can generate distinct network architectures and how this can impact the physiology of an organism. This work defines a model to expand our understanding of the 2-aminoacrylate stress response and the differences in metabolic structures and cellular milieus between S. enterica and E. coli.
Copyright © 2017 American Society for Microbiology.

Entities:  

Keywords:  2-aminoacrylate; PLP-dependent enzymes; RidA; metabolic network structure

Mesh:

Substances:

Year:  2017        PMID: 28461448      PMCID: PMC5494748          DOI: 10.1128/JB.00140-17

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  54 in total

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Journal:  Nucleic Acids Res       Date:  2000-01-01       Impact factor: 16.971

Review 2.  Principles for the buffering of genetic variation.

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3.  A member of the YER057c/yjgf/Uk114 family links isoleucine biosynthesis and intact mitochondria maintenance in Saccharomyces cerevisiae.

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Journal:  Genes Cells       Date:  2001-06       Impact factor: 1.891

4.  L-2,3-diaminopropionate generates diverse metabolic stresses in Salmonella enterica.

Authors:  Dustin C Ernst; Mary E Anderson; Diana M Downs
Journal:  Mol Microbiol       Date:  2016-05-06       Impact factor: 3.501

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Authors:  R R Rando
Journal:  Biochemistry       Date:  1974-09-10       Impact factor: 3.162

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Authors:  W E Balch; R S Wolfe
Journal:  Appl Environ Microbiol       Date:  1976-12       Impact factor: 4.792

7.  Exposure of Escherichia coli and Salmonella enterica serovar Typhimurium to triclosan induces a species-specific response, including drug detoxification.

Authors:  Andrew M Bailey; Chrystala Constantinidou; Al Ivens; Mark I Garvey; Mark A Webber; Nick Coldham; Jon L Hobman; John Wain; Martin J Woodward; Laura J V Piddock
Journal:  J Antimicrob Chemother       Date:  2009-09-16       Impact factor: 5.790

8.  Decreased coenzyme A levels in ridA mutant strains of Salmonella enterica result from inactivated serine hydroxymethyltransferase.

Authors:  Jeffrey M Flynn; Melissa R Christopherson; Diana M Downs
Journal:  Mol Microbiol       Date:  2013-07-19       Impact factor: 3.501

9.  Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega.

Authors:  Fabian Sievers; Andreas Wilm; David Dineen; Toby J Gibson; Kevin Karplus; Weizhong Li; Rodrigo Lopez; Hamish McWilliam; Michael Remmert; Johannes Söding; Julie D Thompson; Desmond G Higgins
Journal:  Mol Syst Biol       Date:  2011-10-11       Impact factor: 11.429

10.  Adaptive evolution of the lactose utilization network in experimentally evolved populations of Escherichia coli.

Authors:  Selwyn Quan; J Christian J Ray; Zakari Kwota; Trang Duong; Gábor Balázsi; Tim F Cooper; Russell D Monds
Journal:  PLoS Genet       Date:  2012-01-12       Impact factor: 5.917

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  15 in total

Review 1.  RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.

Authors:  Jessica L Irons; Kelsey Hodge-Hanson; Diana M Downs
Journal:  Microbiol Mol Biol Rev       Date:  2020-07-15       Impact factor: 11.056

Review 2.  Reactive Enamines and Imines In Vivo: Lessons from the RidA Paradigm.

Authors:  Andrew J Borchert; Dustin C Ernst; Diana M Downs
Journal:  Trends Biochem Sci       Date:  2019-05-15       Impact factor: 13.807

3.  Increased Activity of Cystathionine β-Lyase Suppresses 2-Aminoacrylate Stress in Salmonella enterica.

Authors:  Dustin C Ernst; Melissa R Christopherson; Diana M Downs
Journal:  J Bacteriol       Date:  2018-04-09       Impact factor: 3.490

4.  Analyses of variants of the Ser/Thr dehydratase IlvA provide insight into 2-aminoacrylate metabolism in Salmonella enterica.

Authors:  Andrew J Borchert; Diana M Downs
Journal:  J Biol Chem       Date:  2018-10-16       Impact factor: 5.157

5.  The Cysteine Desulfurase IscS Is a Significant Target of 2-Aminoacrylate Damage in Pseudomonas aeruginosa.

Authors:  Ronnie L Fulton; Jessica Irons; Diana M Downs
Journal:  mBio       Date:  2022-06-02       Impact factor: 7.786

6.  PA5339, a RidA Homolog, Is Required for Full Growth in Pseudomonas aeruginosa.

Authors:  Jessica Irons; Kelsey M Hodge-Hanson; Diana M Downs
Journal:  J Bacteriol       Date:  2018-10-23       Impact factor: 3.490

7.  Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism.

Authors:  Genny Degani; Alberto Barbiroli; Luca Regazzoni; Laura Popolo; Maria Antonietta Vanoni
Journal:  Int J Mol Sci       Date:  2018-03-22       Impact factor: 5.923

8.  Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.

Authors:  Kelsey M Hodge-Hanson; Diana M Downs
Journal:  PLoS One       Date:  2017-09-28       Impact factor: 3.240

9.  Endogenously generated 2-aminoacrylate inhibits motility in Salmonella enterica.

Authors:  Andrew J Borchert; Diana M Downs
Journal:  Sci Rep       Date:  2017-10-11       Impact factor: 4.379

10.  Mmf1p Couples Amino Acid Metabolism to Mitochondrial DNA Maintenance in Saccharomyces cerevisiae.

Authors:  Dustin C Ernst; Diana M Downs
Journal:  mBio       Date:  2018-02-27       Impact factor: 7.867

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