@article{2351,
  keywords = {Quorum Sensing, Repressor Proteins, Lactones, Phosphorylation, Receptors, Cell Surface, Homoserine, Pentanes, Adenosine Triphosphate, Enterobacteriaceae, Escherichia coli Proteins, Magnetic Resonance Spectroscopy, Mass Spectrometry},
  author = {Karina Xavier and Stephen Miller and Wenyun Lu and Jeong Kim and Joshua Rabinowitz and Istv{\'a}n Pelczer and Martin Semmelhack and Bonnie Bassler},
  title = {Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria.},
  abstract = { <p>Quorum sensing is a process of chemical communication that bacteria use to assess cell population density and synchronize behavior on a community-wide scale. Communication is mediated by signal molecules called autoinducers. The LuxS autoinducer synthase produces 4,5-dihydroxy-2,3-pentanedione (DPD), the precursor to a set of interconverting molecules that are generically called autoinducer-2 (AI-2). In enteric bacteria, AI-2 production induces the assembly of a transport apparatus (called the LuxS regulated (Lsr) transporter) that internalizes endogenously produced AI-2 as well as AI-2 produced by other bacterial species. AI-2 internalization is proposed to be a mechanism enteric bacteria employ to interfere with the signaling capabilities of neighboring species of bacteria. We have previously shown that Salmonella enterica serovar Typhimurium binds a specific cyclic derivative of DPD. Here we show that following internalization, the kinase LsrK phosphorylates carbon-5 of the open form of DPD. Phosphorylated DPD (P-DPD) binds specifically to the repressor of the lsr operon, LsrR, consistent with P-DPD being the inducer of the lsr operon. Subsequently, LsrG catalyzes the cleavage of P-DPD producing 2-phosphoglycolic acid. This series of chemical events is proposed to enable enteric bacteria to respond to the presence of competitor bacteria by sequestering and destroying AI-2, thereby eliminating the competitors{\textquoteright} intercellular communication capabilities.</p> },
  year = {2007},
  journal = {ACS Chem Biol},
  volume = {2},
  pages = {128-36},
  month = {2007 Feb 20},
  issn = {1554-8937},
  doi = {10.1021/cb600444h},
  language = {eng},
}