title: The MqsR/MqsA toxin/antitoxin system protects Escherichia coli during bile acid stress.
abstract: Toxin/antitoxin (TA) systems are ubiquitous within bacterial genomes, and the mechanisms of many TA systems are well characterized. As such, several roles for TA systems have been proposed, such as phage inhibition, gene regulation and persister cell formation. However, the significance of these roles is nebulous due to the subtle influence from individual TA systems. For example, a single TA system has only a minor contribution to persister cell formation. Hence, there is a lack of defining physiological roles for individual TA systems. In this study, phenotype assays were used to determine that the MqsR/MqsA type II TA system of Escherichia coli is important for cell growth and tolerance during stress from the bile salt deoxycholate. Using transcriptomics and purified MqsR, we determined that endoribonuclease toxin MqsR degrades YgiS mRNA, which encodes a periplasmic protein that promotes deoxycholate uptake and reduces tolerance to deoxycholate exposure. The importance of reducing YgiS mRNA by MqsR is evidenced by improved growth, reduced cell death and reduced membrane damage when cells without ygiS are stressed with deoxycholate. Therefore, we propose that MqsR/MqsA is physiologically important for E. coli to thrive in the gallbladder and upper intestinal tract, where high bile concentrations are prominent.
authors.affiliation: Department of Chemical Engineering, Pennsylvania State University, University Park, PA, 16802-4400, USA.
authors.forename: Brian W
authors.initials: BW
authors.lastname: Kwan
authors.affiliation: Department of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, RI, 02912, USA.
authors.forename: Dana M
authors.initials: DM
authors.lastname: Lord
authors.affiliation: Department of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, RI, 02912, USA.|Department of Chemistry, Brown University, Providence, RI, 02912, USA.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Peti
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI, 02912, USA.
authors.forename: Rebecca
authors.initials: R
authors.lastname: Page
authors.affiliation: Department of Biology, Texas A & M University, College Station, TX, 77845, USA.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Benedik
authors.affiliation: Department of Chemical Engineering, Pennsylvania State University, University Park, PA, 16802-4400, USA.|Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, 16802-4400, USA.
authors.forename: Thomas K
authors.initials: TK
authors.lastname: Wood
mesh_terms: D001692:Biological Transport / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D003840:Deoxycholic Acid / Q000378:metabolism*; D004722:Endoribonucleases / Q000378:metabolism; D004926:Escherichia coli / Q000254:growth & development*; D029968:Escherichia coli Proteins / Q000235:genetics* / Q000378:metabolism*; D005704:Gallbladder / Q000382:microbiology; D006801:Humans; D007422:Intestines / Q000382:microbiology; D008969:Molecular Sequence Data; D033903:Periplasmic Proteins / Q000235:genetics* / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D013312:Stress, Physiological
chemical_list: D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C555039:MqsA protein, E coli; C508571:MqsR protein, E coli; D033903:Periplasmic Proteins; D012333:RNA, Messenger; C000606950:YgiS protein, E coli; D003840:Deoxycholic Acid; D004722:Endoribonucleases