Engineering an improved light-induced dimer (iLID) for controlling the localization and activity of signaling proteins

The discovery of light-inducible protein-protein interactions has allowed for the spatial and temporal control of a variety of biological processes. To be effective, a photodimerizer should have several characteristics: it should show a large change in binding affinity upon light stimulation, it should not cross-react with other molecules in the cell, and it should be easily used in a variety of organisms to recruit proteins of interest to each other. To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa. In the dark the SsrA peptide is sterically blocked…

• UD
  U.S. Department of Energy
• NI
  National Institutes of Health

  Award: GM093208
• OO
  Office of Science

  Award: W-31-109-Eng-38
• NI
  National Institute of General Medical Sciences

  Award: GM093208
• BE
  Basic Energy Sciences

  Award: W-31-109-Eng-38