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dc.contributor.authorLoddeke, Melissaen_US
dc.contributor.authorSchneider, Barbaraen_US
dc.contributor.authorOguri, Tamikoen_US
dc.contributor.authorMehta, Itien_US
dc.contributor.authorXuan, Zhenyuen_US
dc.contributor.authorReitzer, Lawrence J.en_US
dc.date.accessioned2018-08-24T21:25:16Z
dc.date.available2018-08-24T21:25:16Z
dc.date.created2017-07-25en_US
dc.date.issued2018-08-24
dc.identifier.issn0021-9193en_US
dc.identifier.urihttp://hdl.handle.net/10735.1/6032
dc.descriptionFull text access from Treasures at UT Dallas is available only to current UTD affiliates.en_US
dc.description.abstractSalmonella enterica has two CyuR-activated enzymes that degrade cysteine, i.e., the aerobic CdsH and an unidentified anaerobic enzyme; Escherichia coli has only the latter. To identify the anaerobic enzyme, transcript profiling was performed for E. coli without cyuR and with overexpressed cyuR. Thirty-seven genes showed at least 5-fold changes in expression, and the cyuPA (formerly yhaOM) operon showed the greatest difference. Homology suggested that CyuP and CyuA represent a cysteine transporter and an iron-sulfur-containing cysteine desulfidase, respectively. E. coli and S. enterica Delta cyuA mutants grown with cysteine generated substantially less sulfide and had lower growth yields. Oxygen affected the CyuR-dependent genes reciprocally; cyuP-lacZ expression was greater anaerobically, whereas cdsH-lacZ expression was greater aerobically. In E. coli and S. enterica, anaerobic cyuP expression required cyuR and cysteine and was induced by L-cysteine, D-cysteine, and a few sulfur-containing compounds. Loss of either CyuA or RidA, both of which contribute to cysteine degradation to pyruvate, increased cyuP-lacZ expression, which suggests that CyuA modulates intracellular cysteine concentrations. Phylogenetic analysis showed that CyuA homologs are present in obligate and facultative anaerobes, confirming an anaerobic function, and in archaeal methanogens and bacterial acetogens, suggesting an ancient origin. Our results show that CyuA is the major anaerobic cysteine-catabolizing enzyme in both E. coli and S. enterica, and it is proposed that anaerobic cysteine catabolism can contribute to coordination of sulfur assimilation and amino acid synthesis. IMPORTANCE Sulfur-containing compounds such as cysteine and sulfide are essential and reactive metabolites. Exogenous sulfur-containing compounds can alter the thiol landscape and intracellular redox reactions and are known to affect several cellular processes, including swarming motility, antibiotic sensitivity, and biofilm formation. Cysteine inhibits several enzymes of amino acid synthesis; therefore, increasing cysteine concentrations could increase the levels of the inhibited enzymes. This inhibition implies that control of intracellular cysteine levels, which is the immediate product of sulfide assimilation, can affect several pathways and coordinate metabolism. For these and other reasons, cysteine and sulfide concentrations must be controlled, and this work shows that cysteine catabolism contributes to this control.en_US
dc.description.sponsorship"This work was supported in part by grant GM085536 from the National Institutes of Health."en_US
dc.language.isoenen_US
dc.relation.urihttp://dx.doi.org/10.1128/JB.00117-17
dc.rights©2017 American Society for Microbiologyen_US
dc.sourceJournal of Bacteriology
dc.subjectMetabolismen_US
dc.subjectCysteineen_US
dc.subjectCystathionine gamma-lyaseen_US
dc.subjectEscherichia colien_US
dc.subjectHydrogen Sulfideen_US
dc.subjectSalmonella entericaen_US
dc.titleAnaerobic Cysteine Degradation and Potential Metabolic Coordination in Salmonella Enterica and Escherichia Colien_US
dc.type.genrearticleen_US
dc.description.departmentSchool of Natural Sciences and Mathematicsen_US
dc.description.departmentCenter for Systems Biologyen_US
dc.identifier.bibliographicCitationLoddeke, Melissa, Barbara Schneider, Tamiko Oguri, Iti Mehta, et al. 2017. "Anaerobic Cysteine Degradation and Potential Metabolic Coordination in Salmonella enterica and Escherichia coli." Journal of Bacteriology 199(16), doi:10.1128/JB.00117-17en_US
dc.identifier.volume199en_US
dc.identifier.issue16en_US
dc.contributor.utdAuthorLoddeke, Melissaen_US
dc.contributor.utdAuthorSchneider, Barbaraen_US
dc.contributor.utdAuthorOguri, Tamikoen_US
dc.contributor.utdAuthorMehta, Itien_US
dc.contributor.utdAuthorXuan, Zhenyuen_US
dc.contributor.utdAuthorReitzer, Lawrence J.en_US


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