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. 2014 Jul 1;33(15):1713–1726. doi: 10.15252/embj.201387695

Figure 1. Selection of LOV domains and expression in mammalian cells.

Figure 1

  1. Domain structure of light-sensing proteins from which LOV domains (highlighted with asterisk) were excised (AtPH1 and AtPH2, Arabidopsis thaliana phototropin 1 and 2; CrPH, Chlamydomonas rheinhardtii phototropin; NcVV, Neurospora crassa vivid; NcWC1, N. crassa white collar 1; RsLP, Rhodobacter sphaeroides ATCC 17025 light-sensing protein; VfAU1, Vaucheria frigida aureochrome1). In these proteins, LOV domains regulate a variety of effector domains (STK, serine/threonine kinase; DB, DNA-binding domain). To test for expression and influence on cell viability in mammalian cells, LOV domains optimized for mammalian codon usage were fused to the fluorescent protein mVenus (mV).
  2. Fluorescence intensity measurements of human embryonic kidney (HEK) 293 cells transfected with mVenus-LOV domain fusions.
  3. Viability of HEK293 cells transfected with mVenus-LOV domain fusions.
  4. Fluorescence intensity measurements of Chinese hamster ovary (CHO) K1 cells transfected with mVenus-LOV domain fusions.
  5. Viability of CHO K1 cells transfected with mVenus-LOV domain fusions.

Data information: For (B–E): fluorescence and viability were quantified 16–18 h after transfection. Data were normalized to mV fused to the small, robustly folding FK506 binding protein (FKBP). Mean values ± SD for three independent experiments each performed in quadruplicates are shown.