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@ARTICLE{Budyak:53707,
      author       = {Budyak, I. L. and Pipich, V. and Mironova, O. S. and
                      Schlesinger, R. and Zaccai, G. and Klein-Seetharaman, J.},
      title        = {{S}hape and oligomerization state of the cytoplasmic domain
                      of the phototaxis transducer {II} from {N}atronobacterium
                      pharaonis},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {103},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-53707},
      pages        = {15428 - 15433},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Phototaxis allows archaea to adjust flagellar motion in
                      response to light. In the photophobic response of
                      Natronobacterium pharaonis, light-activated sensory
                      rhodopsin II causes conformational changes in the transducer
                      II protein (pHtrII), initiating the two-component signaling
                      system analogous to bacterial chemotaxis. pHtrII's
                      cytoplasmic domain (pHtrII-cyt) is homologous to the
                      cytoplasmic domains of eubacterial chemotaxis receptors.
                      Chemotaxis receptors require dimerization for activity and
                      are in vivo-organized in large clusters. In this study we
                      investigated the oligomerization and aggregation states of
                      pHtrII-cyt by using chemical cross-linking, analytical
                      gel-filtration chromatography, and small-angle neutron
                      scattering. We show that pHtrII-cyt is monomeric in dilute
                      buffers, but forms dimers in 4 M KCl, the physiological salt
                      concentration for halophilic archaea. At high ammonium
                      sulfate concentration, the protein forms higher-order
                      aggregates. The monomeric protein has a rod-like shape, 202
                      A in length and 14.4 A in diameter; upon dimerization the
                      length increases to 248 A and the diameter to 18.2 A. These
                      results suggest that under high salt concentration the shape
                      and oligomerization state of pHtrII-cyt are comparable to
                      those of chemotaxis receptors.},
      keywords     = {Archaeal Proteins: chemistry / Archaeal Proteins: genetics
                      / Archaeal Proteins: metabolism / Biopolymers: chemistry /
                      Carotenoids: chemistry / Carotenoids: genetics /
                      Carotenoids: metabolism / Cross-Linking Reagents: chemistry
                      / Crystallography, X-Ray / Dimerization / Light /
                      Natronobacterium: chemistry / Natronobacterium: metabolism /
                      Particle Size / Phototrophic Processes: physiology / Protein
                      Structure, Quaternary / Protein Structure, Tertiary /
                      Archaeal Proteins (NLM Chemicals) / Biopolymers (NLM
                      Chemicals) / Cross-Linking Reagents (NLM Chemicals) /
                      phototaxis receptor sensory rhodopsin II, Natronobacterium
                      pharaonis (NLM Chemicals) / Carotenoids (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-2 / IFF-INS / IFF-ISM / Jülich Centre for Neutron
                      Science JCNS (JCNS) ; JCNS},
      ddc          = {000},
      cid          = {I:(DE-Juel1)VDB58 / I:(DE-Juel1)VDB341 / I:(DE-Juel1)VDB342
                      / I:(DE-Juel1)JCNS-20121112},
      pnm          = {Funktion und Dysfunktion des Nervensystems / Kondensierte
                      Materie / Großgeräte für die Forschung mit Photonen,
                      Neutronen und Ionen (PNI)},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK414 /
                      G:(DE-Juel1)FUEK415},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17032755},
      pmc          = {pmc:PMC1592645},
      UT           = {WOS:000241476200029},
      doi          = {10.1073/pnas.0607201103},
      url          = {https://juser.fz-juelich.de/record/53707},
}