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@ARTICLE{Mironova:59010,
      author       = {Mironova, O. S. and Budyak, I. L. and Büldt, G. and
                      Schlesinger, R. and Heberle, J.},
      title        = {{FT}-{IR} difference spectroscopy elucidates crucial
                      interactions of sensory rhodopsin {I} with the cognate
                      transducer {H}trl},
      journal      = {Biochemistry},
      volume       = {46},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-59010},
      pages        = {9399 - 9405},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The phototaxis receptor sensory rhodopsin I (SRI) from
                      Halobacterium salinarum interacts with its cognate
                      transducer (HtrI) forming a transmembrane complex. After
                      light excitation of the chromophore all-trans retinal, SRI
                      undergoes structural changes that are ultimately transmitted
                      to HtrI. The interaction of SRI with HtrI results in the
                      closure of the receptor's proton pathway, which renders the
                      photocycle recovery kinetics of SRI pH-independent. We
                      demonstrate on heterologously expressed and reconstituted
                      SRI-HtrI fusion proteins that the transmembrane part of HtrI
                      (residues 1-52) as well as the downstream cytoplasmic part
                      (residues 53-147) exhibit conformational changes after light
                      excitation. The sum of these conformational changes is
                      similar to those observed in the fusion constructs SRI-HtrI
                      1-71 and SRI-HtrI 1-147, which display pH-independent
                      receptor kinetics. These results indicate the occurrence of
                      spatially distinct conformational changes that are required
                      for functional signal transmission. Kinetic and
                      spectroscopic analysis of HtrI point mutants of Asn53
                      provides evidence that this residue is involved in the
                      receptor-transducer interaction. We suggest that Asn53 plays
                      a role similar to that of Asn74 of the HtrII from
                      Natronobacterium pharaonis, the latter forming a hydrogen
                      bond to the receptor within the membrane.},
      keywords     = {Archaeal Proteins: chemistry / Archaeal Proteins: genetics
                      / Archaeal Proteins: radiation effects / Asparagine:
                      chemistry / Asparagine: genetics / Halorhodopsins: chemistry
                      / Halorhodopsins: genetics / Halorhodopsins: radiation
                      effects / Light / Membrane Proteins: chemistry / Membrane
                      Proteins: genetics / Membrane Proteins: radiation effects /
                      Point Mutation / Protein Interaction Mapping / Recombinant
                      Fusion Proteins: chemistry / Recombinant Fusion Proteins:
                      genetics / Recombinant Fusion Proteins: radiation effects /
                      Sensory Rhodopsins: chemistry / Sensory Rhodopsins: genetics
                      / Sensory Rhodopsins: radiation effects / Spectroscopy,
                      Fourier Transform Infrared / Archaeal Proteins (NLM
                      Chemicals) / Halorhodopsins (NLM Chemicals) / Membrane
                      Proteins (NLM Chemicals) / Recombinant Fusion Proteins (NLM
                      Chemicals) / SRI protein, Halobacterium (NLM Chemicals) /
                      Sensory Rhodopsins (NLM Chemicals) / htrI protein,
                      Halobacterium salinarium (NLM Chemicals) / Asparagine (NLM
                      Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17655327},
      UT           = {WOS:000248692400005},
      doi          = {10.1021/bi700563f},
      url          = {https://juser.fz-juelich.de/record/59010},
}