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000005168 084__ $$2WoS$$aBiochemistry & Molecular Biology
000005168 084__ $$2WoS$$aBiophysics
000005168 1001_ $$0P:(DE-Juel1)VDB60877$$aKriegsmann, J.$$b0$$uFZJ
000005168 245__ $$aSensory rhodopsin II/transducer complex formation in detergent and in lipid bilayers studied with FRET
000005168 260__ $$aAmsterdam$$bElsevier$$c2009
000005168 300__ $$a522 - 531
000005168 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000005168 440_0 $$019423$$aBBA - Biomembranes$$v1788$$x0005-2736$$y2
000005168 500__ $$aJ. F. thanks G. Buldt (Forschungszentrum Julich) for continuous and sustainable support in his institute. This work was supported by the Deutsche Forschungsgerneinschaft (M.E.) and by a priority program SPP 1128 of Deutsche Forschungsgerneinschaft (FI 841/3-1,2 to J.F.). We are indebted to R. Schlesinger for providing us with bacteriorhodopsin and to R. Batra-Safferling for the discussions and comments on the manuscript.
000005168 520__ $$aThe photophobic receptor from Natronomonas pharaonis (NpSRII) forms a photo-signalling complex with its cognate transducer (NpHtrII). In order to elucidate the complex formation in more detail, we have studied the intermolecular binding of both constituents (NpSRII and NpHtrII157; truncated at residue 157) in detergent buffers, and in lipid bilayers using FRET. The data for hetero-dimer formation of NpSRII/NpHtrII in detergent agrees well with KD values (approximately 200 nM) described in the literature. In lipid bilayers, the binding affinity between proteins in the NpSRII/NpHtrII complex is at least one order of magnitude stronger. In detergent the strength of binding is similar for both homo-dimers (NpSRII/NpSRII and NpHtrII/NpHtrII) but significantly weaker (KD approximately 16 microM) when compared to the hetero-dimer. The intermolecular binding is again considerably stronger in lipid bilayers; however, it is not as strong as that observed for the hetero-dimer. At a molar transducer/lipid ratio of 1:2000, which is still well above physiological concentrations, only 40% homo-dimers are formed. Apparently, in cell membranes the formation of the assumed functionally active oligomeric 2:2 complex depends on the full-length transducer including the helical cytoplasmic part, which is thought to tighten the transducer-dimer association.
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000005168 65320 $$2Author$$aFluorescence spectroscopy
000005168 65320 $$2Author$$aLipid vesicle
000005168 65320 $$2Author$$aPhoto signalling
000005168 65320 $$2Author$$aSensory rhodopsin
000005168 65320 $$2Author$$aMembrane protein interaction
000005168 65320 $$2Author$$aDissociation constant
000005168 650_2 $$2MeSH$$aArchaeal Proteins: chemistry
000005168 650_2 $$2MeSH$$aArchaeal Proteins: genetics
000005168 650_2 $$2MeSH$$aArchaeal Proteins: metabolism
000005168 650_2 $$2MeSH$$aBiophysical Phenomena
000005168 650_2 $$2MeSH$$aDetergents
000005168 650_2 $$2MeSH$$aHalobacteriaceae: chemistry
000005168 650_2 $$2MeSH$$aHalobacteriaceae: genetics
000005168 650_2 $$2MeSH$$aHalobacteriaceae: metabolism
000005168 650_2 $$2MeSH$$aLipid Bilayers: chemistry
000005168 650_2 $$2MeSH$$aModels, Molecular
000005168 650_2 $$2MeSH$$aProtein Binding
000005168 650_2 $$2MeSH$$aProtein Multimerization
000005168 650_2 $$2MeSH$$aProtein Structure, Quaternary
000005168 650_2 $$2MeSH$$aSensory Rhodopsins: chemistry
000005168 650_2 $$2MeSH$$aSensory Rhodopsins: genetics
000005168 650_2 $$2MeSH$$aSensory Rhodopsins: metabolism
000005168 650_2 $$2MeSH$$aSignal Transduction
000005168 650_2 $$2MeSH$$aSpectrophotometry
000005168 650_7 $$00$$2NLM Chemicals$$aArchaeal Proteins
000005168 650_7 $$00$$2NLM Chemicals$$aDetergents
000005168 650_7 $$00$$2NLM Chemicals$$aHtrII protein, Natronobacterium pharaonis
000005168 650_7 $$00$$2NLM Chemicals$$aLipid Bilayers
000005168 650_7 $$00$$2NLM Chemicals$$aSensory Rhodopsins
000005168 650_7 $$2WoSType$$aJ
000005168 7001_ $$0P:(DE-Juel1)VDB77075$$aBrehs, M.$$b1$$uFZJ
000005168 7001_ $$0P:(DE-HGF)0$$aKlare, J.P.$$b2
000005168 7001_ $$0P:(DE-HGF)0$$aEngelhard, M.$$b3
000005168 7001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b4$$uFZJ
000005168 773__ $$0PERI:(DE-600)2209384-9$$a10.1016/j.bbamem.2008.11.011$$gVol. 1788, p. 522 - 531$$p522 - 531$$q1788<522 - 531$$tBiochimica et biophysica acta / Biomembranes$$v1788$$x0005-2736$$y2009
000005168 8567_ $$uhttp://dx.doi.org/10.1016/j.bbamem.2008.11.011
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