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@ARTICLE{Fettweiss:850885,
      author       = {Fettweiss, Timo and Röllen, Katrin and Granzin, Joachim
                      and Reiners, Oliver and Endres, Stephan and Drepper, Thomas
                      and Willbold, Dieter and Jaeger, Karl-Erich and
                      Batra-Safferling, Renu and Krauss, Ulrich},
      title        = {{M}echanistic {B}asis of the {F}ast {D}ark {R}ecovery of
                      the {S}hort {LOV} {P}rotein {D}s{LOV} from {D}inoroseobacter
                      shibae},
      journal      = {Biochemistry},
      volume       = {57},
      number       = {32},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2018-04636},
      pages        = {4833–4847},
      year         = {2018},
      abstract     = {Light, oxygen, voltage (LOV) proteins, a ubiquitously
                      distributed class of photoreceptors, regulate a wide variety
                      of light-dependent physiological responses. Because of their
                      modular architecture, LOV domains, i.e., the sensory domains
                      of LOV photoreceptors, have been widely used for the
                      construction of optogenetic tools. We recently described the
                      structure and function of a short LOV protein (DsLOV) from
                      the marine phototropic bacterium Dinoroseobacter shibae, for
                      which, in contrast to other LOV photoreceptors, the dark
                      state represents the physiologically relevant signaling
                      state. Among bacterial LOV photoreceptors, DsLOV possesses
                      an exceptionally fast dark recovery, corroborating its
                      function as a "dark" sensor. To address the mechanistic
                      basis of this unusual characteristic, we performed a
                      comprehensive mutational, kinetic, thermodynamic, and
                      structural characterization of DsLOV. The mechanistic basis
                      of the fast dark recovery of the protein was revealed by
                      mutation of the previously noted uncommon residue
                      substitution at position 49 found in DsLOV. The substitution
                      of M49 with different residues that are naturally conserved
                      in LOV domains tuned the dark-recovery time of DsLOV over 3
                      orders of magnitude, without grossly affecting its overall
                      structure or the light-dependent structural change observed
                      for the wild-type protein. Our study thus provides a
                      striking example of how nature can achieve LOV photocycle
                      tuning by subtle structural alterations in the LOV domain
                      active site, highlighting the easy evolutionary adaptability
                      of the light sensory function. At the same time, our data
                      provide guidance for the mutational photocycle tuning of LOV
                      domains, with relevance for the growing field of
                      optogenetics.},
      cin          = {ICS-6 / IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)IMET-20090612},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29989797},
      UT           = {WOS:000442184600008},
      doi          = {10.1021/acs.biochem.8b00645},
      url          = {https://juser.fz-juelich.de/record/850885},
}