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@ARTICLE{Kriegsmann:5168,
      author       = {Kriegsmann, J. and Brehs, M. and Klare, J.P. and Engelhard,
                      M. and Fitter, J.},
      title        = {{S}ensory rhodopsin {II}/transducer complex formation in
                      detergent and in lipid bilayers studied with {FRET}},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1788},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-5168},
      pages        = {522 - 531},
      year         = {2009},
      note         = {J. 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.},
      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.},
      keywords     = {Archaeal Proteins: chemistry / Archaeal Proteins: genetics
                      / Archaeal Proteins: metabolism / Biophysical Phenomena /
                      Detergents / Halobacteriaceae: chemistry / Halobacteriaceae:
                      genetics / Halobacteriaceae: metabolism / Lipid Bilayers:
                      chemistry / Models, Molecular / Protein Binding / Protein
                      Multimerization / Protein Structure, Quaternary / Sensory
                      Rhodopsins: chemistry / Sensory Rhodopsins: genetics /
                      Sensory Rhodopsins: metabolism / Signal Transduction /
                      Spectrophotometry / Archaeal Proteins (NLM Chemicals) /
                      Detergents (NLM Chemicals) / HtrII protein, Natronobacterium
                      pharaonis (NLM Chemicals) / Lipid Bilayers (NLM Chemicals) /
                      Sensory Rhodopsins (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19094962},
      UT           = {WOS:000263794700025},
      doi          = {10.1016/j.bbamem.2008.11.011},
      url          = {https://juser.fz-juelich.de/record/5168},
}