@article{3771,
  keywords = {Gene Expression Regulation, Bacterial, Quorum Sensing, Repressor Proteins, Escherichia coli, DNA-Binding Proteins, Viral Proteins, Bacteriophages, Lysogeny, Genes, Viral, Prophages, Viral Regulatory and Accessory Proteins},
  author = {Justin Silpe and Andrew Bridges and Xiuliang Huang and Daniela Coronado and Olivia Duddy and Bonnie Bassler},
  title = {Separating Functions of the Phage-Encoded Quorum-Sensing-Activated Antirepressor Qtip.},
  abstract = { <p>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 (cI), leading to host-cell lysis. Here, we show that Qtip interacts with the N terminus of~cI, inhibiting both cI DNA binding and cI autoproteolysis. Qtip also sequesters cI, localizing it to the poles. Qtip can localize to the poles independently of cI. Alanine-scanning mutagenesis of Qtip shows that its localization and interference with cI 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.</p> },
  year = {2020},
  journal = {Cell Host Microbe},
  volume = {27},
  pages = {629-641.e4},
  month = {2020 Apr 08},
  issn = {1934-6069},
  doi = {10.1016/j.chom.2020.01.024},
  language = {eng},
}