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• W2000496147 abstract "The photophobic receptor from Natronomonas pharaonis (NpSRII) forms a photo-signalling complex with its cognate transducer (NpHtrII). In order to elucidate the complex formation in more detail, we have studied the intermolecular binding of both constituents (NpSRII and NpHtrII157; truncated at residue 157) in detergent buffers, and in lipid bilayers using FRET. The data for hetero-dimer formation of NpSRII/NpHtrII in detergent agrees well with KD values (approximately 200 nM) described in the literature. In lipid bilayers, the binding affinity between proteins in the NpSRII/NpHtrII complex is at least one order of magnitude stronger. In detergent the strength of binding is similar for both homo-dimers (NpSRII/NpSRII and NpHtrII/NpHtrII) but significantly weaker (KD approximately 16 microM) when compared to the hetero-dimer. The intermolecular binding is again considerably stronger in lipid bilayers; however, it is not as strong as that observed for the hetero-dimer. At a molar transducer/lipid ratio of 1:2000, which is still well above physiological concentrations, only 40% homo-dimers are formed. Apparently, in cell membranes the formation of the assumed functionally active oligomeric 2:2 complex depends on the full-length transducer including the helical cytoplasmic part, which is thought to tighten the transducer-dimer association." @default.
• W2000496147 created "2016-06-24" @default.
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• W2000496147 date "2009-02-01" @default.
• W2000496147 modified "2023-10-18" @default.
• W2000496147 title "Sensory rhodopsin II/transducer complex formation in detergent and in lipid bilayers studied with FRET" @default.
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• W2000496147 doi "https://doi.org/10.1016/j.bbamem.2008.11.011" @default.
• W2000496147 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19094962" @default.
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