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@ARTICLE{Hemmer:917514,
      author       = {Hemmer, Stefanie and Schulte, Marianne and
                      Knieps-Grünhagen, Esther and Granzin, Joachim and Willbold,
                      Dieter and Jaeger, Karl-Erich and Batra-Safferling, Renu and
                      Panwalkar, Vineet and Krauss, Ulrich},
      title        = {{R}esidue alterations within a conserved hydrophobic pocket
                      influence light, oxygen, voltage photoreceptor dark
                      recovery},
      journal      = {Photochemical $\&$ photobiological sciences},
      volume       = {22},
      issn         = {1474-905X},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {FZJ-2023-00727},
      pages        = {713-727},
      year         = {2023},
      abstract     = {Light, oxygen, voltage (LOV) photoreceptors are widely
                      distributed throughout all kingdoms of life, and have in
                      recent years, due to their modular nature, been broadly used
                      as sensor domains for the construction of optogenetic tools.
                      For understanding photoreceptor function as well as for
                      optogenetic tool design and fine-tuning, a detailed
                      knowledge of the photophysics, photochemistry, and
                      structural changes underlying the LOV signaling paradigm is
                      instrumental. Mutations that alter the lifetime of the
                      photo-adduct signaling state represent a convenient handle
                      to tune LOV sensor on/off kinetics and, thus, steady-state
                      on/off equilibria of the photoreceptor (or optogenetic
                      switch). Such mutations, however, should ideally only
                      influence sensor kinetics, while being benign with regard to
                      the nature of the structural changes that are induced by
                      illumination, i.e., they should not result in a disruption
                      of signal transduction. In the present study, we identify a
                      conserved hydrophobic pocket for which mutations have a
                      strong impact on the adduct-state lifetime across different
                      LOV photoreceptor families. Using the slow cycling bacterial
                      short LOV photoreceptor PpSB1-LOV, we show that the I48T
                      mutation within this pocket, which accelerates adduct
                      rupture, is otherwise structurally and mechanistically
                      benign, i.e., light-induced structural changes, as probed by
                      NMR spectroscopy and X-ray crystallography, are not altered
                      in the variant. Additional mutations within the pocket of
                      PpSB1-LOV and the introduction of homologous mutations in
                      the LOV photoreceptor YtvA of Bacillus subtilis and the
                      Avena sativa LOV2 domain result in similarly altered
                      kinetics. Given the conserved nature of the corresponding
                      structural region, the here identified mutations should find
                      application in dark-recovery tuning of optogenetic tools and
                      LOV photoreceptors, alike.},
      cin          = {IBG-1 / IMET / IBI-7},
      ddc          = {620},
      cid          = {I:(DE-Juel1)IBG-1-20101118 / I:(DE-Juel1)IMET-20090612 /
                      I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / 2171 - Biological and environmental resources
                      for sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36480084},
      UT           = {WOS:000895631300002},
      doi          = {10.1007/s43630-022-00346-5},
      url          = {https://juser.fz-juelich.de/record/917514},
}