TY - JOUR
T1 - Regulation of LuxPQ receptor activity by the quorum-sensing signal autoinducer-2
AU - Neiditch, Matthew B.
AU - Federle, Michael J.
AU - Miller, Stephen T.
AU - Bassler, Bonnie Lynn
AU - Hughson, Frederick McLaury
N1 - Funding Information:
We gratefully acknowledge Michael Becker and the staff of the National Synchrotron Light Source X25 beamline for assistance with X-ray data collection; Kenny Mok, Audra Pompeani, Jennifer Rosenbluth, Boryana Rossenova, Jacob Thomas, and Kim Tu for experimental contributions; Yigong Shi, Tom Silhavy, and Jeff Stock for critical review of the manuscript; and Shawn Campagna, Martin Semmelhack, Tom Silhavy, Jeff Stock, Peter Wolanin, and members of our laboratories for advice and discussion. This work was supported by National Institutes of Health (NIH) grants AI-054442 and GM-065859 as well as NIH postdoctoral fellowships (to M.B.N. and M.J.F.).
PY - 2005/5/27
Y1 - 2005/5/27
N2 - 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.
AB - 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.
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U2 - 10.1016/j.molcel.2005.04.020
DO - 10.1016/j.molcel.2005.04.020
M3 - Article
C2 - 15916958
AN - SCOPUS:19444366428
SN - 1097-2765
VL - 18
SP - 507
EP - 518
JO - Molecular Cell
JF - Molecular Cell
IS - 5
ER -