title: A qrr noncoding RNA deploys four different regulatory mechanisms to optimize quorum-sensing dynamics.
abstract: Quorum sensing is a cell-cell communication process that bacteria use to transition between individual and social lifestyles. In vibrios, homologous small RNAs called the Qrr sRNAs function at the center of quorum-sensing pathways. The Qrr sRNAs regulate multiple mRNA targets including those encoding the quorum-sensing regulatory components luxR, luxO, luxM, and aphA. We show that a representative Qrr, Qrr3, uses four distinct mechanisms to control its particular targets: the Qrr3 sRNA represses luxR through catalytic degradation, represses luxM through coupled degradation, represses luxO through sequestration, and activates aphA by revealing the ribosome binding site while the sRNA itself is degraded. Qrr3 forms different base-pairing interactions with each mRNA target, and the particular pairing strategy determines which regulatory mechanism occurs. Combined mathematical modeling and experiments show that the specific Qrr regulatory mechanism employed governs the potency, dynamics, and competition of target mRNA regulation, which in turn, defines the overall quorum-sensing response.
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
authors.forename: Lihui
authors.initials: L
authors.lastname: Feng
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
authors.forename: Steven T
authors.initials: ST
authors.lastname: Rutherford
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
authors.forename: Kai
authors.initials: K
authors.lastname: Papenfort
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
authors.forename: John D
authors.initials: JD
authors.lastname: Bagert
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
authors.forename: Julia C
authors.initials: JC
authors.lastname: van Kessel
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
authors.forename: David A
authors.initials: DA
authors.lastname: Tirrell
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. Electronic address: wingreen@princeton.edu.
authors.forename: Ned S
authors.initials: NS
authors.lastname: Wingreen
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA. Electronic address: bbassler@princeton.edu.
authors.forename: Bonnie L
authors.initials: BL
authors.lastname: Bassler
mesh_terms: D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics; D055029:Inverted Repeat Sequences; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D053038:Quorum Sensing; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D058727:RNA, Small Untranslated / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014733:Vibrio / Q000235:genetics / Q000378:metabolism*
chemical_list: D012329:RNA, Bacterial; D012333:RNA, Messenger; D058727:RNA, Small Untranslated