Ligand Binding Kinetics of the Quorum Sensing Regulator PqsR

Martin Welch, James T. Hodgkinson, Jeremy Gross, David R. Spring, Thomas Sams

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The Pseudomonas aeruginosa quinolone signal (PQS) is a quorum sensing molecule that plays an important role in regulating the virulence of this organism. We have purified the ligand binding domain of the receptor PqsRLBD for PQS and have used Förster resonance energy transfer fluorimetry and kinetic modeling to characterize the ligand binding in vitro. The dissociation constant for binding of PQS to a ligand binding site in (PqsRLBD)2 dimers was determined to be 1.2 ± 0.3 μM. We found no cooperativity in the consecutive binding of two ligand molecules to the dimer.
Original languageEnglish
JournalBiochemistry
Volume52
Issue number25
Pages (from-to)4433-4438
ISSN0006-2960
DOIs
Publication statusPublished - 2013

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