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@ARTICLE{Rani:137277,
      author       = {Rani, Raj and Jentzsch, Katrin and Lecher, Justin and
                      Hartmann, Rudolf and Willbold, Dieter and Jaeger, Karl-Erich
                      and Krauss, Ulrich},
      title        = {{C}onservation of {D}ark {R}ecovery {K}inetic {P}arameters
                      and {S}tructural {F}eatures in the {P}seudomonadaceae
                      “{S}hort” {L}ight, {O}xygen, {V}oltage ({LOV}) {P}rotein
                      {F}amily: {I}mplications for the {D}esign of {LOV}-{B}ased
                      {O}ptogenetic {T}ools},
      journal      = {Biochemistry},
      volume       = {52},
      number       = {26},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2013-03734},
      pages        = {4460 - 4473},
      year         = {2013},
      abstract     = {In bacteria and fungi, various light, oxygen, voltage (LOV)
                      sensory systems that lack a fused effector domain but
                      instead contain only short N- and C-terminal extensions
                      flanking the LOV core exist. In the prokaryotic kingdom,
                      this so-called “short” LOV protein family represents the
                      third largest LOV photoreceptor family. This observation
                      prompted us to study their distribution and phylogeny as
                      well as their photochemical and structural properties in
                      more detail. We recently described the slow and fast
                      reverting “short” LOV proteins PpSB1-LOV and PpSB2-LOV
                      from Pseudomonas putida KT2440 whose adduct state lifetimes
                      varied by 3 orders of magnitude [Jentzsch, K., Wirtz, A.,
                      Circolone, F., Drepper, T., Losi, A., Gärtner, W., Jaeger,
                      K. E., and Krauss, U. (2009) Biochemistry 48,
                      10321–10333]. We now present evidence of the conservation
                      of similar fast and slow-reverting “short” LOV proteins
                      in different Pseudomonas species. Truncation studies
                      conducted with PpSB1-LOV and PpSB2-LOV suggested that the
                      short N- and C-terminal extensions outside of the LOV core
                      domain are essential for the structural integrity and
                      folding of the two proteins. While circular dichroism and
                      solution nuclear magnetic resonance experiments verify that
                      the two short C-terminal extensions of PpSB1-LOV and
                      PpSB2-LOV form independently folding helical structures in
                      solution, bioinformatic analyses imply the formation of
                      coiled coils of the respective structural elements in the
                      context of the dimeric full-length proteins. Given their
                      prototypic architecture, conserved in most more complex LOV
                      photoreceptor systems, “short” LOV proteins could
                      represent ideally suited building blocks for the design of
                      genetically encoded photoswitches (i.e., LOV-based
                      optogenetic tools).},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000321522800003},
      doi          = {10.1021/bi400311r},
      url          = {https://juser.fz-juelich.de/record/137277},
}