The Regulation of Histidine Sensor Kinase Complexes by Quorum Sensing Signal Molecules

Matthew B. Neiditch, Frederick M. Hughson

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations

Abstract

Two-component sensor kinase signaling systems are widespread in bacteria, but gaining mechanistic insight into how kinase activity is controlled by ligand binding has proved challenging. Here, we discuss this problem in the context of our structural and functional studies of bacterial quorum sensing receptors. Specifically, this chapter focuses on the transmembrane sensor kinase complex LuxPQ, which serves as the receptor for the "universal" quorum sensing signal molecule autoinducer-2 (AI-2). Methods are presented for the overproduction, purification, crystallization, and functional characterization of LuxPQ's ligand-binding (periplasmic) domain.

Original languageEnglish (US)
Title of host publicationTwo Component Signaling Systems, Part B
PublisherAcademic Press Inc.
Pages250-263
Number of pages14
DOIs
StatePublished - Jan 1 2007

Publication series

NameMethods in Enzymology
Volume423
ISSN (Print)0076-6879

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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    Neiditch, M. B., & Hughson, F. M. (2007). The Regulation of Histidine Sensor Kinase Complexes by Quorum Sensing Signal Molecules. In Two Component Signaling Systems, Part B (pp. 250-263). (Methods in Enzymology; Vol. 423). Academic Press Inc.. https://doi.org/10.1016/S0076-6879(07)23011-3