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@ARTICLE{Mennes:57377,
      author       = {Mennes, N. and Klare, J. P. and Chizhov, I. and Seidel, R.
                      and Schlesinger, R. and Engelhard, M.},
      title        = {{E}xpression of the halobacterial transducer protein
                      {H}tr{II} from {N}atronomonas pharaonis in {E}scherichia
                      coli},
      journal      = {FEBS letters},
      volume       = {581},
      issn         = {0014-5793},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-57377},
      pages        = {1487 - 1494},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Archaeal phototaxis is mediated by sensory rhodopsins which
                      form complexes with their cognate transducers. Whereas the
                      receptors sensory rhodopsin I and sensory rhodopsin II
                      (SRII) have been expressed in Escherichia coli (E. coli)
                      only shortened fragments of HtrII from Natronomonas
                      pharaonis (NpHtrII) are available. Here we describe the
                      heterologous expression of full length NpHtrII which was
                      achieved in yields of up to 0.9 mg per litre cell culture.
                      Gel filtration analysis reveals the tendency of the
                      transducer to form dimers and higher-order oligomers which
                      was also observed when complexed to NpSRII. A circular
                      dichroism (CD) spectrum of NpHtrII is comparable to those
                      obtained for the E. coli chemoreceptors indicating a similar
                      folding with predominantly alpha-helical structure. NpHtrII
                      dissociates from the NpSRII/HtrII complex with an apparent
                      K(D) of about 0.6 microM. Photocycle kinetics of the complex
                      is comparable to that obtained for NpSRII in complex with a
                      truncated transducer with slight differences in the M-decay.
                      The data indicate that the heterologously expressed NpHtrII
                      adopt a native like structure, providing the means for
                      elucidating transmembrane signal transduction and activation
                      of microbial signalling cascades.},
      keywords     = {Archaeal Proteins: biosynthesis / Archaeal Proteins:
                      chemistry / Archaeal Proteins: isolation $\&$ purification /
                      Chromatography, Gel / Circular Dichroism / Cloning,
                      Molecular / Dimerization / Escherichia coli: genetics /
                      Lasers / Photolysis / Protein Structure, Secondary /
                      Recombinant Proteins: biosynthesis / Recombinant Proteins:
                      chemistry / Recombinant Proteins: isolation $\&$
                      purification / Archaeal Proteins (NLM Chemicals) / HtrII
                      protein, Natronobacterium pharaonis (NLM Chemicals) /
                      Recombinant Proteins (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 / Biophysics / Cell
                      Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17368449},
      UT           = {WOS:000245913300036},
      doi          = {10.1016/j.febslet.2007.03.005},
      url          = {https://juser.fz-juelich.de/record/57377},
}