Tuning Chemoreceptor Signaling by Positioning Aromatic Residues at the Lipid–Aqueous Interface
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 that other research groups find it useful to modulate signal output from their receptor of interest.
KeywordsAromatic tuning Stimulus-independent signaling Signal output modulation Signal pathway mapping Polar–hydrophobic interfaces Membrane–protein interactions
R.Y. was generously supported by the Indonesia Endowment Fund for Education, Ministry of Finance (S-4833/LPDP.3/2015). R.J.L. and L.V.E. received support from the University of Portsmouth. R.R.D. was supported with start-up funding from the Faculty of Science and from the Institute of Biological and Biomolecular Science (IBBS) at the University of Portsmouth.
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