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Probing the sensory rhodopsin II binding domain of its cognate transducer by calorimetry and electrophysiology

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Schmies,  Georg
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Nagel,  Georg
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Bamberg,  Ernst
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Hippler-Mreyen, S., Klare, J. P., Wegener, A. A., Seidel, R., Herrman, C., Schmies, G., et al. (2003). Probing the sensory rhodopsin II binding domain of its cognate transducer by calorimetry and electrophysiology. Journal of Molecular Biology (London), 330(5), 1203-1213. doi:10.1016/s0022-2836(03)00656-9.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DBDA-A
Abstract
Sensory rhodopsin II, a repellent phototaxis receptor from Natronobacterium pharaonis (NpSRII) forms a tight complex with its cognate transducer (NpHtrII). Light excitation of the receptor triggers conformational changes in both proteins, thereby activating the cellular two-component signalling cascade. In membranes, the two proteins form a 2:2 complex, which dissociates to a 1:1 heterodimer in micelles. Complexed to the transducer sensory rhodopsin II is no longer capable of light-driven proton pumping. In order to elucidate the dimerisation and the size of the receptor-binding domain of the transducer, isothermal titration calorimetry and electrophysiological experiments have been carried out. It is shown, that an N-terminal sequence of 114 amino acid residues is sufficient for tight binding (Kd=240nM; DeltaH=-17.6kJmol-1) and for inhibiting the proton transfer. These data and results obtained from selected site-directed mutants indicate a synergistic interplay of transducer transmembrane domain (1-82) and cytoplasmic peptide (83-114) leading to an optimal and specific interaction between receptor and transducer.