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Separating Functions of the Phage-Encoded Quorum-Sensing-Activated Antirepressor Qtip.
Silpe, Justin E; Bridges, Andrew A; Huang, Xiuliang; Coronado, Daniela R; Duddy, Olivia P; Bassler, Bonnie L.
Afiliación
  • Silpe JE; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
  • Bridges AA; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA.
  • Huang X; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA.
  • Coronado DR; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
  • Duddy OP; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
  • Bassler BL; Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA. Electronic address: bbassler@princeton.edu.
Cell Host Microbe ; 27(4): 629-641.e4, 2020 04 08.
Article en En | MEDLINE | ID: mdl-32101705
Quorum sensing is a process of chemical communication that bacteria use to track cell density and coordinate gene expression across a population. Bacteria-infecting viruses, called phages, can encode quorum-sensing components that enable them to integrate host cell density information into the lysis-lysogeny decision. Vibriophage VP882 is one such phage, and activation of its quorum-sensing pathway leads to the production of an antirepressor called Qtip. Qtip interferes with the prophage repressor (cIVP882), leading to host-cell lysis. Here, we show that Qtip interacts with the N terminus of cIVP882, inhibiting both cIVP882 DNA binding and cIVP882 autoproteolysis. Qtip also sequesters cIVP882, localizing it to the poles. Qtip can localize to the poles independently of cIVP882. Alanine-scanning mutagenesis of Qtip shows that its localization and interference with cIVP882 activities are separable. Comparison of Qtip to a canonical phage antirepressor reveals that despite both proteins interacting with their partner repressors, only Qtip drives polar localization.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Represoras / Bacteriófagos / Percepción de Quorum / Proteínas Reguladoras y Accesorias Virales Tipo de estudio: Prognostic_studies Idioma: En Revista: Cell Host Microbe Asunto de la revista: MICROBIOLOGIA Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Represoras / Bacteriófagos / Percepción de Quorum / Proteínas Reguladoras y Accesorias Virales Tipo de estudio: Prognostic_studies Idioma: En Revista: Cell Host Microbe Asunto de la revista: MICROBIOLOGIA Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos