TY - CHAP
T1 - Tuning chemoreceptor signaling by positioning aromatic residues at the lipid-aqueous interface
AU - Yusuf, Rahmi
AU - Lawrence, Robert
AU - Eke, Lucy
AU - Draheim, Roger
PY - 2018/2/11
Y1 - 2018/2/11
N2 - 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.
AB - 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.
KW - aromatic tuning
KW - stimulus-independent signaling
KW - signal output modulation
KW - signal pathway mapping
KW - polar/hydrophobic interfaces
KW - membrane-protein interactions
U2 - 10.1007/978-1-4939-7577-8_14
DO - 10.1007/978-1-4939-7577-8_14
M3 - Chapter (peer-reviewed)
VL - 1729
T3 - Methods in Molecular Biology
BT - Bacterial Chemosensing
PB - Springer
ER -