Tuning chemoreceptor signaling by positioning aromatic residues at the lipid-aqueous interface

Rahmi Yusuf, Robert Lawrence, Lucy Eke, Roger Draheim

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)peer-review

Abstract

Aromatic tuning facilitates stimulus-independent modulation of receptor output. The methodology is based upon the affinity of amphipathic aromatic residues, namely Trp and Tyr, for the polar/hydrophobic interfaces found within biological membranes. Here, we describe the application of aromatic tuning within the aspartate chemoreceptor of Escherichia coli (Tar). We have also employed the method within other related proteins, such as sensor histidine kinases (SHKs), and therefore hope other research groups find it useful to modulate signal output from their receptor of interest.
Original languageEnglish
Title of host publicationBacterial Chemosensing
PublisherSpringer
Volume1729
DOIs
Publication statusEarly online - 11 Feb 2018

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
ISSN (Print)1064-3745

Keywords

  • aromatic tuning
  • stimulus-independent signaling
  • signal output modulation
  • signal pathway mapping
  • polar/hydrophobic interfaces
  • membrane-protein interactions

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