title: Antimicrobial peptides trigger a division block in Escherichia coli through stimulation of a signalling system.
abstract: Antimicrobial peptides are an important component of the molecular arsenal employed by hosts against bacteria. Many bacteria in turn possess pathways that provide protection against these compounds. In Escherichia coli and related bacteria, the PhoQ/PhoP signalling system is a key regulator of this antimicrobial peptide defence. Here we show that treating E. coli with sublethal concentrations of antimicrobial peptides causes cells to filament, and that this division block is controlled by the PhoQ/PhoP system. The filamentation results from increased expression of QueE, an enzyme that is part of a tRNA modification pathway but that, as we show here, also affects cell division. We also find that a functional YFP-QueE fusion localizes to the division septum in filamentous cells, suggesting QueE blocks septation through interaction with the divisome. Regulation of septation by PhoQ/PhoP may protect cells from antimicrobial peptide-induced stress or other conditions associated with high-level stimulation of this signalling system.
authors.affiliation: Department of Biology, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Srujana S
authors.initials: SS
authors.lastname: Yadavalli
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Jeffrey N
authors.identifier: 0000-0002-5105-0265
authors.initials: JN
authors.lastname: Carey
authors.affiliation: Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Rachel S
authors.initials: RS
authors.lastname: Leibman
authors.affiliation: Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Annie I
authors.initials: AI
authors.lastname: Chen
authors.affiliation: Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Andrew M
authors.initials: AM
authors.lastname: Stern
authors.affiliation: Department of Biology, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Manuela
authors.initials: M
authors.lastname: Roggiani
authors.affiliation: Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Andrew M
authors.initials: AM
authors.lastname: Lippa
authors.affiliation: Department of Biology, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.|Department of Physics, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Mark
authors.initials: M
authors.lastname: Goulian
mesh_terms: D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D053898:Biosynthetic Pathways / Q000187:drug effects; D002455:Cell Division / Q000187:drug effects / Q000235:genetics; D020090:Chromosome Segregation / Q000187:drug effects; D003593:Cytoplasm / Q000187:drug effects / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D008954:Models, Biological; D009704:Nucleoside Q / Q000096:biosynthesis; D015398:Signal Transduction / Q000187:drug effects*; D014158:Transcription, Genetic / Q000187:drug effects
chemical_list: D023181:Antimicrobial Cationic Peptides; D029968:Escherichia coli Proteins; C576029:PhoQ protein, E coli; D009704:Nucleoside Q