Regulation of LuxPQ receptor activity by the quorum-sensing signal autoinducer-2

Matthew B. Neiditch, Michael J. Federle, Stephen T. Miller, Bonnie Lynn Bassler, Frederick McLaury Hughson

Research output: Contribution to journalArticle

135 Scopus citations

Abstract

The extracellular signaling molecule autoinducer-2 (AI-2) mediates quorum-sensing communication in diverse bacterial species. In marine vibrios, binding of AI-2 to the periplasmic receptor LuxP modulates the activity of the inner membrane sensor kinase LuxQ, transducing the AI-2 information into the cytoplasm. Here, we show that Vibrio harveyi LuxP associates with LuxQ in both the presence and absence of AI-2. The 1.9 Å X-ray crystal structure of apoLuxP, complexed with the periplasmic domain of LuxQ, reveals that the latter contains two tandem Per/ARNT/Simple-minded (PAS) folds. Thus, although many prokaryotic PAS folds themselves bind ligands, the LuxQ periplasmic PAS folds instead bind LuxP, monitoring its AI-2 occupancy. Mutations that disrupt the apoLuxP:LuxQ interface sensitize V. harveyi to AI-2, implying that AI-2 binding causes the replacement of one set of LuxP:LuxQ contacts with another. These conformational changes switch LuxQ between two opposing enzymatic activities, each of which conveys information to the cytoplasm about the cell density of the surrounding environment.

Original languageEnglish (US)
Pages (from-to)507-518
Number of pages12
JournalMolecular Cell
Volume18
Issue number5
DOIs
StatePublished - May 27 2005

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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